1k5w

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Revision as of 16:45, 20 November 2007

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THREE-DIMENSIONAL STRUCTURE OF THE SYNAPTOTAGMIN 1 C2B-DOMAIN: SYNAPTOTAGMIN 1 AS A PHOSPHOLIPID BINDING MACHINE

Overview

Synaptotagmin 1 probably functions as a Ca2+ sensor in neurotransmitter, release via its two C2-domains, but no common Ca2+-dependent activity that, could underlie a cooperative action between them has been described. The, NMR structure of the C2B-domain now reveals a beta sandwich that exhibits, striking similarities and differences with the C2A-domain. Whereas the, bottom face of the C2B-domain has two additional alpha helices that may be, involved in specialized Ca2+-independent functions, the top face binds two, Ca2+ ions and is remarkably similar to the C2A-domain. Consistent with, these results, but in contrast to previous studies, we find that the, C2B-domain binds phospholipids in a Ca2+-dependent manner similarly to the, C2A-domain. These results suggest a novel view of synaptotagmin function, whereby the two C2-domains cooperate in a common activity, Ca2+-dependent, phospholipid binding, to trigger neurotransmitter release.

About this Structure

1K5W is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine., Fernandez I, Arac D, Ubach J, Gerber SH, Shin O, Gao Y, Anderson RG, Sudhof TC, Rizo J, Neuron. 2001 Dec 20;32(6):1057-69. PMID:11754837

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