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PDBsum entry 2mf9
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Apoptosis, isomerase
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PDB id
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2mf9
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References listed in PDB file
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Key reference
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Title
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Functional role of the flexible n-Terminal extension of fkbp38 in catalysis.
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Authors
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C.Kang,
H.Ye,
J.Chia,
B.H.Choi,
S.Dhe-Paganon,
B.Simon,
U.Schütz,
M.Sattler,
H.S.Yoon.
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Ref.
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Sci Rep, 2013,
3,
2985.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Backbone 1h, 13c, And 15n resonance assignments of the n-Terminal domain of fkbp38 (fkbp38ntd).
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Authors
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C.B.Kang,
H.Ye,
S.Vivekanandan,
B.Simon,
M.Sattler,
H.S.Yoon.
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Ref.
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J Biomol Nmr, 2006,
36,
37.
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PubMed id
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