View source for 5hzh


==Crystal structure of photoinhibitable Rac1 containing C450A mutant LOV2 domain==
<StructureSection load='5hzh' size='340' side='right'caption='[[5hzh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hzh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Avena_sativa Avena sativa] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HZH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5hzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hzh OCA], [https://pdbe.org/5hzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hzh RCSB], [https://www.ebi.ac.uk/pdbsum/5hzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hzh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RAC1_HUMAN RAC1_HUMAN] Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref>   Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.<ref>PMID:1643658</ref> <ref>PMID:9121475</ref> <ref>PMID:19934221</ref> <ref>PMID:19403692</ref> <ref>PMID:20696765</ref> [https://www.uniprot.org/uniprot/O49003_AVESA O49003_AVESA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets of signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder of diverse proteins, thereby generating robust allosteric switches. Sensory domains were inserted into nonconserved, surface-exposed loops that were tight and identified computationally as allosterically coupled to active sites. Allosteric switches introduced into motility signaling proteins (kinases, guanosine triphosphatases, and guanine exchange factors) controlled conversion between conformations closely resembling natural active and inactive states, as well as modulated the morphodynamics of living cells. Our results illustrate a broadly applicable approach to design physiological protein switches.

Engineering extrinsic disorder to control protein activity in living cells.,Dagliyan O, Tarnawski M, Chu PH, Shirvanyants D, Schlichting I, Dokholyan NV, Hahn KM Science. 2016 Dec 16;354(6318):1441-1444. PMID:27980211<ref>PMID:27980211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hzh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Rac 3D structures|Rac 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Avena sativa]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chu PH]]
[[Category: Dagliyan O]]
[[Category: Dokholyan NV]]
[[Category: Hahn KM]]
[[Category: Schlichting I]]
[[Category: Shirvanyants D]]
[[Category: Tarnawski M]]