3bxj
From Proteopedia
(Difference between revisions)
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<StructureSection load='3bxj' size='340' side='right'caption='[[3bxj]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3bxj' size='340' side='right'caption='[[3bxj]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3bxj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXJ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxj OCA], [https://pdbe.org/3bxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxj RCSB], [https://www.ebi.ac.uk/pdbsum/3bxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxj OCA], [https://pdbe.org/3bxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxj RCSB], [https://www.ebi.ac.uk/pdbsum/3bxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SYGP1_RAT SYGP1_RAT] Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits.<ref>PMID:15312654</ref> <ref>PMID:15500970</ref> <ref>PMID:16537406</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bxj ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bxj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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 Apr;9(4):350-5. Epub 2008 Mar 7. PMID:18323856<ref>PMID:18323856</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3bxj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ahmadian | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Bonneau | + | [[Category: Ahmadian MR]] |
| - | [[Category: Eberth | + | [[Category: Bonneau F]] |
| - | [[Category: Gremer | + | [[Category: Eberth A]] |
| - | [[Category: Hothorn | + | [[Category: Gremer L]] |
| - | [[Category: Kaschau | + | [[Category: Hothorn M]] |
| - | [[Category: Parret | + | [[Category: Kaschau N]] |
| - | [[Category: Pena | + | [[Category: Parret A]] |
| - | [[Category: Scheffzek | + | [[Category: Pena V]] |
| - | + | [[Category: Scheffzek K]] | |
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Current revision
Crystal Structure of the C2-GAP Fragment of synGAP
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Categories: Large Structures | Rattus norvegicus | Ahmadian MR | Bonneau F | Eberth A | Gremer L | Hothorn M | Kaschau N | Parret A | Pena V | Scheffzek K
