2mf9: Difference between revisions

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==Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)==
==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=''>
<StructureSection load='2mf9' size='340' side='right'caption='[[2mf9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mf9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mf9]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF9 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP8, FKBP38 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf9 OCA], [https://pdbe.org/2mf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf9 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf9 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2mf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf9 OCA], [https://pdbe.org/2mf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf9 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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>
[https://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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Kang C]]
[[Category: Kang, C]]
[[Category: Sattler M]]
[[Category: Sattler, M]]
[[Category: Simon B]]
[[Category: Simon, B]]
[[Category: Ye H]]
[[Category: Ye, H]]
[[Category: Yoon HS]]
[[Category: Yoon, H S]]
[[Category: Apoptosis]]
[[Category: Beta barrel]]
[[Category: Central helix]]
[[Category: Flexible n-terminal extension]]
[[Category: Isomerase]]

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