2mf9: Difference between revisions
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<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=2mf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mf9 RCSB], [http://www.ebi.ac.uk/pdbsum/2mf9 PDBsum]</span></td></tr> | <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=2mf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mf9 RCSB], [http://www.ebi.ac.uk/pdbsum/2mf9 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[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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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 02:07, 25 December 2014
Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)
Structural highlights
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] Publication Abstract from PubMedFKBP38 regulates apoptosis through unique interactions with multiple regulators including Bcl-2. Interestingly, the peptidylprolyl isomerase activity of FKBP38 is only detectable when it binds to calcium-saturated calmodulin (CaM/Ca(2+)). This, in turn, permits the formation of a complex with Bcl-2. FKBP38 thereby provides an important link between isomerase activity and apoptotic pathways. Here, we show that the N-terminal extension (residues 1-32) preceding the catalytic domain of FKBP38 has an autoinhibitory activity. The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain. Notably, CaM/Ca(2+) binds to this N-terminal extension and thereby releases the autoinhibitory contacts between the N-terminal extension and the catalytic domain, thus potentiating the isomerase activity of FKBP38. Our data demonstrate how CaM/Ca(2+) modulates the catalytic activity of FKBP38. Functional role of the flexible N-terminal extension of FKBP38 in catalysis.,Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schutz U, Sattler M, Yoon HS Sci Rep. 2013 Oct 22;3:2985. doi: 10.1038/srep02985. PMID:24145868[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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