3feh: Difference between revisions
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==Crystal structure of full length centaurin alpha-1== | |||
<StructureSection load='3feh' size='340' side='right'caption='[[3feh]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3feh]] 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=3FEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FEH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3feh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3feh OCA], [https://pdbe.org/3feh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3feh RCSB], [https://www.ebi.ac.uk/pdbsum/3feh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3feh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ADAP1_HUMAN ADAP1_HUMAN] GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).<ref>PMID:10448098</ref> <ref>PMID:10333475</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin alpha1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule. | |||
Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1.,Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110<ref>PMID:21057110</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3feh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: Bochkarev | [[Category: Arrowsmith CH]] | ||
[[Category: Bountra | [[Category: Bochkarev A]] | ||
[[Category: Edwards | [[Category: Bountra C]] | ||
[[Category: MacKenzie | [[Category: Edwards AM]] | ||
[[Category: Park | [[Category: MacKenzie F]] | ||
[[Category: Park H]] | |||
[[Category: Shen | [[Category: Shen L]] | ||
[[Category: Tempel | [[Category: Tempel W]] | ||
[[Category: Tong | [[Category: Tong Y]] | ||
[[Category: Weigelt | [[Category: Weigelt J]] | ||
Latest revision as of 09:33, 6 December 2023
Crystal structure of full length centaurin alpha-1
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