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2r83

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|PDB= 2r83 |SIZE=350|CAPTION= <scene name='initialview01'>2r83</scene>, resolution 2.70&Aring;
|PDB= 2r83 |SIZE=350|CAPTION= <scene name='initialview01'>2r83</scene>, resolution 2.70&Aring;
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+101'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Residue+A+102'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+A+103'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+A+104'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+A+105'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+B+106'>AC6</scene>, <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+B+107'>AC7</scene> and <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+A+108'>AC8</scene>
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+101'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Residue+A+102'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+A+103'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+A+104'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+A+105'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+B+106'>AC6</scene>, <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+B+107'>AC7</scene> and <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+A+108'>AC8</scene>
-
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
+
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= SYT1, SVP65, SYT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= SYT1, SVP65, SYT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r83 OCA], [http://www.ebi.ac.uk/pdbsum/2r83 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2r83 RCSB]</span>
}}
}}
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[[Category: Robert, J J]]
[[Category: Robert, J J]]
[[Category: Sutton, R B.]]
[[Category: Sutton, R B.]]
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[[Category: CL]]
 
[[Category: c2a-c2b]]
[[Category: c2a-c2b]]
[[Category: calcium]]
[[Category: calcium]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:33:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:57:28 2008''

Revision as of 01:57, 31 March 2008

Image:2r83.jpg


PDB ID 2r83

Drag the structure with the mouse to rotate
, resolution 2.70Å
Sites: , , , , , , and
Ligands:
Gene: SYT1, SVP65, SYT (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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