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  • Binding Sites  (4)
  • Guanine nucleotide binding protein  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Distribution and relative levels of expression of the phosphoinositidase-C-linked G-proteins G"qα and G"1"1α: Absence of G"1"1α in human platelets and haemopoietically derived cell lines
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1179 (1993), S. 208-212 
    Details
    ISSN: 0167-4889
    Keywords: Co-expression ; Guanine nucleotide binding protein ; Immunoblotting ; Inositol lipid ; Phospholipase C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4889(93)90143-D
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunological identification of the α subunit of G13, a novel guanine nucleotide binding protein
    Amsterdam : Elsevier
    FEBS Letters 297 (1992), S. 186-188 
    Details
    ISSN: 0014-5793
    Keywords: Guanine nucleotide binding protein ; Signal transduction
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)80357-M
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The α"2 B adrenergic receptor of undifferentiated neuroblastoma x glioma hybrid NG108-15 cells, interacts directly with the guanine nucleotide binding protein, G"i2
    Amsterdam : Elsevier
    FEBS Letters 269 (1990), S. 430-434 
    Details
    ISSN: 0014-5793
    Keywords: Anti-peptide antiserum ; Guanine nucleotide binding protein ; Pertussis toxin ; α"2B Adrenergic receptor
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(90)81209-7
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The human muscarinic M1 acetylcholine receptor, when expressed in CHO cells, activates and downregulates both G"qα and G"1"1α equally and non-selectively
    Amsterdam : Elsevier
    FEBS Letters 324 (1993), S. 241-245 
    Details
    ISSN: 0014-5793
    Keywords: Guanine nucleotide binding protein ; Inositol trisphosphate ; Muscarinic acetylcholine receptor ; Phospholipase C
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81401-K
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  • 5
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    The way things move: looking under the hood of molecular motor proteins (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-07
    Description: The microtubule-based kinesin motors and actin-based myosin motors generate motions associated with intracellular trafficking, cell division, and muscle contraction. Early studies suggested that these molecular motors work by very different mechanisms. Recently, however, it has become clear that kinesin and myosin share a common core structure and convert energy from adenosine triphosphate into protein motion using a similar conformational change strategy. Many different types of mechanical amplifiers have evolved that operate in conjunction with the conserved core. This modular design has given rise to a remarkable diversity of kinesin and myosin motors whose motile properties are optimized for performing distinct biological functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vale, R D -- Milligan, R A -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):88-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA. vale@phy.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10753125" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Cytoskeleton/metabolism ; Evolution, Molecular ; Kinesin/chemistry/*physiology ; Microtubules/metabolism ; Models, Biological ; Models, Molecular ; Molecular Motor Proteins/chemistry/*physiology ; Myosins/chemistry/*physiology ; Protein Conformation ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-09
    Description: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    Structure and functional role of dynein's microtubule-binding domain (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-12-17
    Description: Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2663340/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2663340/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, Andrew P -- Garbarino, Joan E -- Wilson-Kubalek, Elizabeth M -- Shipley, Wesley E -- Cho, Carol -- Milligan, Ronald A -- Vale, Ronald D -- Gibbons, I R -- GM30401-29/GM/NIGMS NIH HHS/ -- GM52468/GM/NIGMS NIH HHS/ -- P01 AR042895/AR/NIAMS NIH HHS/ -- P01 AR042895-15/AR/NIAMS NIH HHS/ -- P01-AR42895/AR/NIAMS NIH HHS/ -- P41 RR-17573/RR/NCRR NIH HHS/ -- R01 GM097312/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Dec 12;322(5908):1691-5. doi: 10.1126/science.1164424.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19074350" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Dyneins/*chemistry/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Image Processing, Computer-Assisted ; Mice ; Microscopy, Electron ; Microtubules/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Movement ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Structure of the actin-myosin complex and its implications for muscle contraction (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-02
    Description: Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rayment, I -- Holden, H M -- Whittaker, M -- Yohn, C B -- Lorenz, M -- Holmes, K C -- Milligan, R A -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):58-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Wisconsin, Madison 53705.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316858" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*chemistry/metabolism ; Actomyosin/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Image Processing, Computer-Assisted ; *Models, Molecular ; *Muscle Contraction ; Myosin Subfragments/*chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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