4dxa

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dxa]] 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=4DXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXA FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dxa]] 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=4DXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.95&#8491;</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=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</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=4dxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxa OCA], [https://pdbe.org/4dxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxa RCSB], [https://www.ebi.ac.uk/pdbsum/4dxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxa 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=4dxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxa OCA], [https://pdbe.org/4dxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxa RCSB], [https://www.ebi.ac.uk/pdbsum/4dxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RAP1B_HUMAN RAP1B_HUMAN]] GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction.<ref>PMID:20332120</ref> <ref>PMID:18660803</ref>
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[https://www.uniprot.org/uniprot/RAP1B_HUMAN RAP1B_HUMAN] GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction.<ref>PMID:20332120</ref> <ref>PMID:18660803</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cerebral cavernous malformations (CCM) affect 0.1-0.5% of the population resulting in leaky vasculature and severe neurological defects. KRIT1 (Krev interaction trapped-1) mutations associate with ~40% of familial CCM. KRIT1 is an effector of Ras-related protein 1 (Rap1) GTPase. Rap1 relocalizes KRIT1 from microtubules to cell membranes to impact integrin activation, potentially important for CCM pathology. We report the 1.95A co-crystal structure of KRIT1 FERM domain in complex with Rap1. Rap1-KRIT1 interaction encompasses an extended surface, including Rap1 Switch I and II and KRIT1 FERM F1 and F2 lobes. Rap1 binds KRIT1-F1 lobe using a GTPase-ubiquitin-like fold interaction, but binds KRIT1-F2 lobe by a novel interaction. Point mutagenesis confirms the interaction. High similarity between KRIT1-F2/F3 and Talin is revealed. Additionally, the mechanism for FERM domains acting as GTPase effectors is suggested. Finally, structure-based alignment of each lobe suggests classification of FERM domains as ERM-like and TMFK-like (Talin-Myosin-FAK-Krit-like) and that FERM lobes resemble domain ''modules''.
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Structural basis for the small G-protein-effector interaction of Ras-related protein 1 (Rap1) and the adaptor protein Krev interaction trapped 1 (KRIT1).,Li X, Zhang R, Draheim KM, Liu W, Calderwood DA, Boggon TJ J Biol Chem. 2012 May 10. PMID:22577140<ref>PMID:22577140</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 4dxa" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==

Current revision

Co-crystal structure of Rap1 in complex with KRIT1

PDB ID 4dxa

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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