2r83

From Proteopedia

Revision as of 06:21, 13 February 2008

Crystal structure analysis of human synaptotagmin 1 C2A-C2B

Overview

Release of neurotransmitter from synaptic vesicles requires the, Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable, evidence that cooperation between the tandem C2 domains of synaptotagmin, is a requirement of regulated exocytosis; however, high-resolution, structural evidence for this interaction has been lacking. The 2.7 A, crystal structure of the cytosolic domains of human synaptotagmin 1 in the, absence of Ca2+ reveals a novel closed conformation of the protein. The, shared interface between C2A and C2B is stabilized by a network of, interactions between residues on the C-terminal alpha-helix of the C2B, domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These, interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel, regulatory mechanism whereby one C2 domain could regulate the other until, an appropriate triggering event decouples them.

About this Structure

2R83 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.

Reference

Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association., Fuson KL, Montes M, Robert JJ, Sutton RB, Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:17956130

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