2esw: Difference between revisions

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-[[Image:2esw.gif|left|200px]]
- {{Structure
+==Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor==
-|PDB= 2esw |SIZE=350|CAPTION= <scene name='initialview01'>2esw</scene>, resolution 2.01&Aring;
+<StructureSection load='2esw' size='340' side='right'caption='[[2esw]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
+<table><tr><td colspan='2'>[[2esw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ESW FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=2esw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2esw OCA], [https://pdbe.org/2esw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2esw RCSB], [https://www.ebi.ac.uk/pdbsum/2esw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2esw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARHG7_MOUSE ARHG7_MOUSE] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity).<ref>PMID:17093062</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2esw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2esw ConSurf].
+<div style="clear:both"></div>
-'''Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor'''
+==See Also==
+*[[Rho guanine nucleotide exchange factor 3D structures|Rho guanine nucleotide exchange factor 3D structures]]
+== References ==
-==Overview==
+<references/>
-The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3(2)21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact beta-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse betaPIX-SH3 domain binding the way in which the betaPIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse betaPIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse betaPIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of betaPIX-SH3 domain resulting in its multiple biological functions.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-ESW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESW OCA].
-==Reference==
-Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor., Li X, Liu X, Sun F, Gao J, Zhou H, Gao GF, Bartlam M, Rao Z, Biochem Biophys Res Commun. 2006 Jan 6;339(1):407-14. Epub 2005 Nov 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16307729 16307729]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Rao Z]]
-[[Category: Rao, Z.]]
-[[Category: CL]]
-[[Category: HG]]
-[[Category: beta barrel]]
-[[Category: sh3 domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:03 2008''