5hvk

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Current revision (08:58, 23 October 2024) (edit) (undo)
 
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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=5hvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hvk OCA], [https://pdbe.org/5hvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hvk RCSB], [https://www.ebi.ac.uk/pdbsum/5hvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hvk 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=5hvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hvk OCA], [https://pdbe.org/5hvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hvk RCSB], [https://www.ebi.ac.uk/pdbsum/5hvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hvk ProSAT]</span></td></tr>
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== Disease ==
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[https://www.uniprot.org/uniprot/LIMK1_HUMAN LIMK1_HUMAN] Williams syndrome. Note=LIMK1 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref>
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[https://www.uniprot.org/uniprot/LIMK1_HUMAN LIMK1_HUMAN] Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Activated by upstream kinases including ROCK1, PAK1 and PAK4, which phosphorylate LIMK1 on a threonine residue located in its activation loop. LIMK1 subsequently phosphorylates and inactivates the actin binding/depolymerizing factors cofilin-1/CFL1, cofilin-2/CFL2 and destrin/DSTN, thereby preventing the cleavage of filamentous actin (F-actin), and stabilizing the actin cytoskeleton. In this way LIMK1 regulates several actin-dependent biological processes including cell motility, cell cycle progression, and differentiation. Phosphorylates TPPP on serine residues, thereby promoting microtubule disassembly. Stimulates axonal outgrowth and may be involved in brain development. Isoform 3 has a dominant negative effect on actin cytoskeletal changes.<ref>PMID:10196227</ref> <ref>PMID:10436159</ref> <ref>PMID:11832213</ref> <ref>PMID:12807904</ref> <ref>PMID:15660133</ref> <ref>PMID:16230460</ref> <ref>PMID:18028908</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Current revision

Crystal structure of LIMK1 mutant D460N in complex with full-length cofilin-1

PDB ID 5hvk

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