2mf9: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
[[2mf9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF9 OCA]. | [[2mf9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jwx 2jwx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF9 OCA]. | ||
==Reference== | ==Reference== | ||
Revision as of 11:12, 13 November 2013
Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)
Template:ABSTRACT PUBMED 24145868
FunctionFunction
[FKBP8_HUMAN] Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis.[1] [2] [3]
About this StructureAbout this Structure
2mf9 is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2jwx. Full experimental information is available from OCA.
ReferenceReference
- ↑ Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schutz U, Sattler M, Yoon HS. Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Sci Rep. 2013 Oct 22;3:2985. doi: 10.1038/srep02985. PMID:24145868 doi:http://dx.doi.org/10.1038/srep02985
- ↑ Shirane M, Nakayama KI. Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat Cell Biol. 2003 Jan;5(1):28-37. PMID:12510191 doi:http://dx.doi.org/10.1038/ncb894
- ↑ Kang CB, Feng L, Chia J, Yoon HS. Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Biochem Biophys Res Commun. 2005 Nov 11;337(1):30-8. PMID:16176796 doi:http://dx.doi.org/S0006-291X(05)02012-7
- ↑ Weiwad M, Edlich F, Erdmann F, Jarczowski F, Kilka S, Dorn M, Pechstein A, Fischer G. A reassessment of the inhibitory capacity of human FKBP38 on calcineurin. FEBS Lett. 2005 Mar 14;579(7):1591-6. PMID:15757646 doi:http://dx.doi.org/S0014-5793(05)00180-8