Publication Date:
1996-07-12
Description:
C2 domains are found in many proteins involved in membrane traffic or signal transduction. Although C2 domains are thought to bind calcium ions, the structural basis for calcium binding is unclear. Analysis of calcium binding to C2 domains of synaptotagmin I and protein kinase C-beta by nuclear magnetic resonance spectroscopy revealed a bipartite calcium-binding motif that involves the coordination of two calcium ions by five aspartate residues located on two separate loops. Sequence comparisons indicated that this may be a widely used calcium-binding motif, designated here as the C2 motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shao, X -- Davletov, B A -- Sutton, R B -- Sudhof, T C -- Rizo, J -- R01-MH52804-01/MH/NIMH NIH HHS/ -- R29 NS33731-01A1/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662510" target="_blank"〉PubMed〈/a〉
Keywords:
Aspartic Acid/chemistry
;
Base Sequence
;
Calcium/*metabolism
;
*Calcium-Binding Proteins
;
Crystallography, X-Ray
;
Hydrogen-Ion Concentration
;
Magnetic Resonance Spectroscopy
;
Membrane Glycoproteins/*chemistry/*metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Nerve Tissue Proteins/*chemistry/*metabolism
;
Phospholipids/metabolism
;
Protein Conformation
;
Protein Folding
;
Protein Kinase C/chemistry/*metabolism
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Synaptotagmin I
;
Synaptotagmins
;
Temperature
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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