1v9d: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V9D FirstGlance]. <br> | <table><tr><td colspan='2'>[[1v9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V9D FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v9d RCSB], [http://www.ebi.ac.uk/pdbsum/1v9d 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=1v9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v9d RCSB], [http://www.ebi.ac.uk/pdbsum/1v9d PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/DIAP1_MOUSE DIAP1_MOUSE]] Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (By similarity).<ref>PMID:9214622</ref> <ref>PMID:10678165</ref> <ref>PMID:15044801</ref> <ref>PMID:18572016</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bugyi, B | [[Category: Bugyi, B]] | ||
[[Category: Geeves, M A | [[Category: Geeves, M A]] | ||
[[Category: Kuhlmann, D | [[Category: Kuhlmann, D]] | ||
[[Category: Narumiya, S | [[Category: Narumiya, S]] | ||
[[Category: Nyitrai, M | [[Category: Nyitrai, M]] | ||
[[Category: Shimada, A | [[Category: Shimada, A]] | ||
[[Category: Vetter, I R | [[Category: Vetter, I R]] | ||
[[Category: Wittinghofer, A | [[Category: Wittinghofer, A]] | ||
[[Category: Helix bundle]] | [[Category: Helix bundle]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||