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3u0r

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Revision as of 22:19, 25 December 2014

Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules

Structural highlights

3u0r 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.
Gene:	API5, MIG8 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[API5_HUMAN] Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Apoptosis inhibitor 5 (API5) is an anti-apoptotic protein that is up-regulated in various cancer cells. Here, we present the crystal structure of human API5. API5 exhibits an elongated all alpha-helical structure. The N-terminal half of API5 is similar to the HEAT repeat and the C-terminal half is similar to the ARM (Armadillo-like) repeat. HEAT and ARM repeats have been implicated in protein-protein interactions, suggesting that the cellular roles of API5 may be to mediate protein-protein interactions. Various components of multiprotein complexes have been identified as API5-interacting protein partners, suggesting that API5 may act as a scaffold for multiprotein complexes. API5 exists as a monomer, and the functionally important heptad leucine repeat does not exhibit the predicted a dimeric leucine zipper. Additionally, Lys-251, which can be acetylated in cells, plays important roles in the inhibition of apoptosis under serum deprivation conditions. The acetylation of this lysine also affects the stability of API5 in cells.

Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules.,Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI J Biol Chem. 2012 Mar 30;287(14):10727-37. doi: 10.1074/jbc.M111.317594. Epub, 2012 Feb 12. PMID:22334682^[4]

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

References

↑ Kim JW, Cho HS, Kim JH, Hur SY, Kim TE, Lee JM, Kim IK, Namkoong SE. AAC-11 overexpression induces invasion and protects cervical cancer cells from apoptosis. Lab Invest. 2000 Apr;80(4):587-94. PMID:10780674
↑ Morris EJ, Michaud WA, Ji JY, Moon NS, Rocco JW, Dyson NJ. Functional identification of Api5 as a suppressor of E2F-dependent apoptosis in vivo. PLoS Genet. 2006 Nov 17;2(11):e196. PMID:17112319 doi:06-PLGE-RA-0285R2
↑ Rigou P, Piddubnyak V, Faye A, Rain JC, Michel L, Calvo F, Poyet JL. The antiapoptotic protein AAC-11 interacts with and regulates Acinus-mediated DNA fragmentation. EMBO J. 2009 Jun 3;28(11):1576-88. doi: 10.1038/emboj.2009.106. Epub 2009 Apr 23. PMID:19387494 doi:10.1038/emboj.2009.106
↑ Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI. Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. J Biol Chem. 2012 Mar 30;287(14):10727-37. doi: 10.1074/jbc.M111.317594. Epub, 2012 Feb 12. PMID:22334682 doi:10.1074/jbc.M111.317594

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/3u0r"

@@ Line 6: / Line 6: @@
 <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=3u0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u0r RCSB], [http://www.ebi.ac.uk/pdbsum/3u0r PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/API5_HUMAN API5_HUMAN]] Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs.<ref>PMID:10780674</ref> <ref>PMID:17112319</ref> <ref>PMID:19387494</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3u0r

From Proteopedia

Revision as of 22:19, 25 December 2014

Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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