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2mf9

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Revision as of 23:04, 9 August 2018

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

Structural highlights

2mf9 is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 2jwx. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	FKBP8, FKBP38 (HUMAN)
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

FKBP38 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.

References

↑ 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
↑ 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 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mf9"

@@ Line 1: / Line 1: @@
 ==Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)==
 <StructureSection load='2mf9' size='340' side='right' caption='[[2mf9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP8, FKBP38 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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://pdbe.org/2mf9 PDBe], [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://pdbe.org/2mf9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mf9 RCSB], [http://www.ebi.ac.uk/pdbsum/2mf9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf9 ProSAT]</span></td></tr>
 </table>
 == Function ==

2mf9

From Proteopedia

Revision as of 23:04, 9 August 2018

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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