2mf9

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'''Unreleased structure'''
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{{STRUCTURE_2mf9| PDB=2mf9 | SCENE= }}
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===Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)===
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{{ABSTRACT_PUBMED_24145868}}
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The entry 2mf9 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/FKBP8_HUMAN 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.<ref>PMID:12510191</ref> <ref>PMID:16176796</ref> <ref>PMID:15757646</ref>
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Authors: Kang, C., Ye, H., Simon, B., Sattler, M., Yoon, H.S.
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==About this Structure==
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[[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].
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Description: Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)
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==Reference==
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<ref group="xtra">PMID:024145868</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Kang, C.]]
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[[Category: Sattler, M.]]
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[[Category: Simon, B.]]
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[[Category: Ye, H.]]
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[[Category: Yoon, H S.]]
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[[Category: Apoptosis]]
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[[Category: Beta barrel]]
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[[Category: Central helix]]
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[[Category: Flexible n-terminal extension]]
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[[Category: Isomerase]]

Revision as of 07:35, 6 November 2013

Template:STRUCTURE 2mf9

Contents

Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)

Template:ABSTRACT PUBMED 24145868

Function

[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 Structure

2mf9 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • 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
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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