3nmx

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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=3nmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nmx RCSB], [http://www.ebi.ac.uk/pdbsum/3nmx PDBsum]</span></td></tr>
<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=3nmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nmx RCSB], [http://www.ebi.ac.uk/pdbsum/3nmx PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ARHG4_HUMAN ARHG4_HUMAN]] Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Binding of APC may activate RAC1 GEF activity. The APC-ARHGEF4 complex seems to be involved in cell migration as well as in E-cadherin-mediated cell-cell adhesion. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression.<ref>PMID:10947987</ref> <ref>PMID:12598901</ref> <ref>PMID:17145773</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 21:39, 25 December 2014

Crystal structure of APC complexed with Asef

3nmx, resolution 2.30Å

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