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3lju

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Revision as of 15:47, 25 December 2014

Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3

Structural highlights

3lju is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	ADAP1, CENTA1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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).^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Venkateswarlu K, Cullen PJ. Molecular cloning and functional characterization of a human homologue of centaurin-alpha. Biochem Biophys Res Commun. 1999 Aug 19;262(1):237-44. PMID:10448098 doi:10.1006/bbrc.1999.1065
↑ Venkateswarlu K, Oatey PB, Tavare JM, Jackson TR, Cullen PJ. Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Biochem J. 1999 Jun 1;340 ( Pt 2):359-63. PMID:10333475
↑ Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW. Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1. Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110 doi:10.1073/pnas.1009008107

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lju"

@@ Line 7: / Line 7: @@
 <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=3lju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lju OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lju RCSB], [http://www.ebi.ac.uk/pdbsum/3lju PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==

3lju

From Proteopedia

Revision as of 15:47, 25 December 2014

Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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