Publication Date:
1999-08-14
Description:
The three-dimensional (3D) structure of the intrinsically dimeric insulin receptor bound to its ligand, insulin, was determined by electron cryomicroscopy. Gold-labeled insulin served to locate the insulin-binding domain. The 3D structure was then fitted with available known high-resolution domain substructures to obtain a detailed contiguous model for this heterotetrameric transmembrane receptor. The 3D reconstruction indicates that the two alpha subunits jointly participate in insulin binding and that the kinase domains in the two beta subunits are in a juxtaposition that permits autophosphorylation of tyrosine residues in the first step of insulin receptor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luo, R Z -- Beniac, D R -- Fernandes, A -- Yip, C C -- Ottensmeyer, F P -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1077-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, M5G 1L6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446056" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
Catalytic Domain
;
Crystallography, X-Ray
;
Dimerization
;
Gold
;
Image Processing, Computer-Assisted
;
Insulin/*chemistry/metabolism
;
Ligands
;
Microscopy, Electron, Scanning Transmission
;
Models, Molecular
;
Phosphorylation
;
Protein Conformation
;
Protein-Tyrosine Kinases/chemistry/metabolism
;
Receptor, Insulin/*chemistry/metabolism
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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