1cf4

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{{Seed}}
 
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[[Image:1cf4.png|left|200px]]
 
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==CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX==
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The line below this paragraph, containing "STRUCTURE_1cf4", creates the "Structure Box" on the page.
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<StructureSection load='1cf4' size='340' side='right'caption='[[1cf4]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1cf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CF4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1cf4| PDB=1cf4 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf4 OCA], [https://pdbe.org/1cf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cf4 RCSB], [https://www.ebi.ac.uk/pdbsum/1cf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cf4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDC42_HUMAN CDC42_HUMAN] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration.<ref>PMID:14978216</ref> <ref>PMID:15642749</ref> <ref>PMID:17038317</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/1cf4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1cf4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The proteins Cdc42 and Rac are members of the Rho family of small GTPases (G proteins), which control signal-transduction pathways that lead to rearrangements of the cell cytoskeleton, cell differentiation and cell proliferation. They do so by binding to downstream effector proteins. Some of these, known as CRIB (for Cdc42/Rac interactive-binding) proteins, bind to both Cdc42 and Rac, such as the PAK1-3 serine/threonine kinases, whereas others are specific for Cdc42, such as the ACK tyrosine kinases and the Wiscott-Aldrich-syndrome proteins (WASPs). The effector loop of Cdc42 and Rac (comprising residues 30-40, also called switch I), is one of two regions which change conformation on exchange of GDP for GTP. This region is almost identical in Cdc42 and Racs, indicating that it does not determine the specificity of these G proteins. Here we report the solution structure of the complex of Cdc42 with the GTPase-binding domain ofACK. Both proteins undergo significant conformational changes on binding, to form a new type of G-protein/effector complex. The interaction extends the beta-sheet in Cdc42 by binding an extended strand from ACK, as seen in Ras/effector interactions, but it also involves other regions of the G protein that are important for determining the specificity of effector binding.
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===CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX===
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Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK.,Mott HR, Owen D, Nietlispach D, Lowe PN, Manser E, Lim L, Laue ED Nature. 1999 May 27;399(6734):384-8. PMID:10360579<ref>PMID:10360579</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1cf4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10360579 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10360579}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1CF4 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF4 OCA].
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==Reference==
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<ref group="xtra">PMID:10360579</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Laue, E D.]]
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[[Category: Large Structures]]
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[[Category: Lim, L.]]
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[[Category: Laue ED]]
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[[Category: Lowe, P N.]]
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[[Category: Lim L]]
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[[Category: Mott, H R.]]
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[[Category: Lowe PN]]
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[[Category: Nietlispach, D.]]
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[[Category: Mott HR]]
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[[Category: Owen, D.]]
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[[Category: Nietlispach D]]
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[[Category: Cdc42/ack gtpase complex]]
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[[Category: Owen D]]
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[[Category: G protein]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:39:05 2009''
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Current revision

CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX

PDB ID 1cf4

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