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4rug

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==Cyrstal structure of SLIT-ROBO Rho GTPase-activating protein 2 fragment==
==Cyrstal structure of SLIT-ROBO Rho GTPase-activating protein 2 fragment==
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<StructureSection load='4rug' size='340' side='right' caption='[[4rug]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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<StructureSection load='4rug' size='340' side='right'caption='[[4rug]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rug]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RUG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RUG FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rtt|4rtt]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rug OCA], [http://pdbe.org/4rug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rug RCSB], [http://www.ebi.ac.uk/pdbsum/4rug PDBsum]</span></td></tr>
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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=4rug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rug OCA], [https://pdbe.org/4rug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rug RCSB], [https://www.ebi.ac.uk/pdbsum/4rug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rug ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/SRGP2_HUMAN SRGP2_HUMAN]] A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13).
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[https://www.uniprot.org/uniprot/SRGP2_HUMAN SRGP2_HUMAN] A chromosomal aberration disrupting SRGAP2 has been found in a patient with early infantile epileptic encephalopathy. Balanced translocation t(1;9)(q32;q13).
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SRGP2_HUMAN SRGP2_HUMAN]] RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.<ref>PMID:20810653</ref> <ref>PMID:21148482</ref> <ref>PMID:22559944</ref>
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[https://www.uniprot.org/uniprot/SRGP2_HUMAN SRGP2_HUMAN] RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral cortex. Its interaction and inhibition by SRGAP2C reduces the rate of spine maturation, alters dendritic spine morphology and density and indirectly increases neuronal migration. It may have implications for cognition, learning and memory. In non-neuronal cells, it may also play a role in cell migration by regulating the formation of lamellipodia and filopodia.<ref>PMID:20810653</ref> <ref>PMID:21148482</ref> <ref>PMID:22559944</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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srGAP proteins regulate cell migration and morphogenesis by shaping the structure and dynamics of the cytoskeleton and membranes. First discovered as intracellular effectors for the Robo1 axon-guidance receptor, srGAPs were later identified as interacting with several other nuclear and cytoplasmic proteins. In all these cases, the srGAP SH3 domain mediates protein-protein interactions by recognizing a short proline-rich segment on the cognate-binding partner. However, as interactions between the isolated SH3 domain and a selected set of ligands show weak affinity and low specificity, it is not clear how srGAPs are precisely recruited to their signaling sites. Here, we report a two-component molecular mechanism that regulates ligand binding to srGAP2 by on the one hand dramatically tightening their association and on the other, moderately autoinhibiting and restricting binding. Our results allow the design of point mutations for better probing of srGAP2 activities, and may facilitate the identification of new srGAP2 ligands.
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The Neuronal Migration Factor srGAP2 Achieves Specificity in Ligand Binding through a Two-Component Molecular Mechanism.,Guez-Haddad J, Sporny M, Sasson Y, Gevorkyan-Airapetov L, Lahav-Mankovski N, Margulies D, Radzimanowski J, Opatowsky Y Structure. 2015 Nov 3;23(11):1989-2000. doi: 10.1016/j.str.2015.08.009. Epub 2015, Sep 10. PMID:26365803<ref>PMID:26365803</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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==See Also==
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</div>
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*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]]
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<div class="pdbe-citations 4rug" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Guez-Hadad, J]]
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[[Category: Homo sapiens]]
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[[Category: Opatowsky, Y]]
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[[Category: Large Structures]]
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[[Category: Ligand binding]]
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[[Category: Guez-Hadad J]]
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[[Category: Nuclear]]
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[[Category: Opatowsky Y]]
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[[Category: Plasma membrane]]
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[[Category: Protein binding]]
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[[Category: Robo1]]
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[[Category: Sh3]]
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[[Category: Srgap2]]
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Current revision

Cyrstal structure of SLIT-ROBO Rho GTPase-activating protein 2 fragment

PDB ID 4rug

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