3bxj

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[[Image:3bxj.jpg|left|200px]]
[[Image:3bxj.jpg|left|200px]]
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{{Structure
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|PDB= 3bxj |SIZE=350|CAPTION= <scene name='initialview01'>3bxj</scene>, resolution 3.0&Aring;
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|GENE= Syngap1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00616 RasGAP], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00323 RasGAP], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00239 C2]</span>
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{{STRUCTURE_3bxj| PDB=3bxj | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxj OCA], [http://www.ebi.ac.uk/pdbsum/3bxj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bxj RCSB]</span>
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'''Crystal Structure of the C2-GAP Fragment of synGAP'''
'''Crystal Structure of the C2-GAP Fragment of synGAP'''
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[[Category: Pena, V.]]
[[Category: Pena, V.]]
[[Category: Scheffzek, K.]]
[[Category: Scheffzek, K.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: gtpase activating protein]]
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[[Category: Gtpase activating protein]]
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[[Category: gtpase activation]]
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[[Category: Gtpase activation]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: phosphoprotein]]
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[[Category: Phosphoprotein]]
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[[Category: sh3-binding]]
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[[Category: Sh3-binding]]
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[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:34:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:29:33 2008''
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Revision as of 06:34, 24 April 2008

Template:STRUCTURE 3bxj

Crystal Structure of the C2-GAP Fragment of synGAP


Overview

The brain-specific synaptic guanosine triphosphatase (GTPase)-activating protein (SynGAP) is important in synaptic plasticity. It shows dual specificity for the small guanine nucleotide-binding proteins Rap and Ras. Here, we show that RapGAP activity of SynGAP requires its C2 domain. In contrast to the isolated GAP domain, which does not show any detectable RapGAP activity, a fragment comprising the C2 and GAP domains (C2-GAP) stimulates the intrinsic GTPase reaction of Rap by approximately 1 x 10(4). The C2-GAP crystal structure, complemented by modelling and biochemical analyses, favours a concerted movement of the C2 domain towards the switch II region of Rap to assist in GTPase stimulation. Our data support a catalytic mechanism similar to that of canonical RasGAPs and distinct from the canonical RapGAPs. SynGAP presents the first example, to our knowledge, of a GAP that uses a second domain for catalytic activity, thus pointing to a new function of C2 domains.

About this Structure

3BXJ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The C2 domain of SynGAP is essential for stimulation of the Rap GTPase reaction., Pena V, Hothorn M, Eberth A, Kaschau N, Parret A, Gremer L, Bonneau F, Ahmadian MR, Scheffzek K, EMBO Rep. 2008 Mar 7;. PMID:18323856 Page seeded by OCA on Thu Apr 24 09:34:13 2008

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