5ybj

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==Structure of apo KANK1 ankyrin domain==
==Structure of apo KANK1 ankyrin domain==
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<StructureSection load='5ybj' size='340' side='right' caption='[[5ybj]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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<StructureSection load='5ybj' size='340' side='right'caption='[[5ybj]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ybj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YBJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ybj]] is a 1 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=5YBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YBJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.341&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KANK1, ANKRD15, KANK, KIAA0172 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=GOL:GLYCEROL'>GOL</scene></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=5ybj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybj OCA], [http://pdbe.org/5ybj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ybj RCSB], [http://www.ebi.ac.uk/pdbsum/5ybj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybj ProSAT]</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=5ybj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybj OCA], [https://pdbe.org/5ybj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ybj RCSB], [https://www.ebi.ac.uk/pdbsum/5ybj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybj ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/KANK1_HUMAN KANK1_HUMAN]] Inherited congenital spastic tetraplegia. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/KANK1_HUMAN KANK1_HUMAN] Inherited congenital spastic tetraplegia. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KANK1_HUMAN KANK1_HUMAN]] Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma.<ref>PMID:16968744</ref> <ref>PMID:18458160</ref> <ref>PMID:19171758</ref> <ref>PMID:22084092</ref>
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[https://www.uniprot.org/uniprot/KANK1_HUMAN KANK1_HUMAN] Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma.<ref>PMID:16968744</ref> <ref>PMID:18458160</ref> <ref>PMID:19171758</ref> <ref>PMID:22084092</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A well-controlled microtubule organization is essential for intracellular transport, cytoskeleton maintenance, and cell development. KN motif and ankyrin repeat domain-containing protein 1 (KANK1), a member of KANK family, could recruit kinesin family member 21A (KIF21A) to the cell cortex to control microtubule growth via its C-terminal ankyrin domain. However, how the KANK1 ankyrin domain recognizes KIF21A and whether other KANK proteins can also bind KIF21A remain unknown. Here, using a combination of structural, site-directed mutagenesis, and biochemical studies, we found that a stretch of ~22 amino acids in KIF21A is sufficient for binding to KANK1 and its close homolog KANK2, and solved the complex structure of the KIF21A peptide with either the KANK1 ankyrin domain or the KANK2 ankyrin domain. In each complex, KIF21A is recognized by two distinct pockets of the ankyrin domain and adopts helical conformations upon binding to the ankyrin domain. The elucidated KANK structures may advance our understanding the role of KANK1 as a scaffolding molecule in controlling microtubule growth at the cell periphery.
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Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins.,Guo Q, Liao S, Zhu Z, Li Y, Li F, Xu C J Biol Chem. 2017 Nov 28. pii: M117.817494. doi: 10.1074/jbc.M117.817494. PMID:29183992<ref>PMID:29183992</ref>
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==See Also==
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*[[Ankyrin repeat domain-containing protein 3D structures|Ankyrin repeat domain-containing protein 3D structures]]
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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 5ybj" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Guo, Q]]
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[[Category: Large Structures]]
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[[Category: Liao, S]]
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[[Category: Guo Q]]
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[[Category: Min, J]]
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[[Category: Liao S]]
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[[Category: Structural genomic]]
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[[Category: Min J]]
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[[Category: Xu, C]]
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[[Category: Xu C]]
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[[Category: Cell adhesion]]
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Current revision

Structure of apo KANK1 ankyrin domain

PDB ID 5ybj

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