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PDBsum entry 2f2p
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Metal binding protein
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PDB id
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2f2p
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References listed in PDB file
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Key reference
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Title
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Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode.
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Authors
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Q.Ye,
X.Li,
A.Wong,
Q.Wei,
Z.Jia.
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Ref.
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Biochemistry, 2006,
45,
738-745.
[DOI no: ]
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PubMed id
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Abstract
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Calcineurin is a calmodulin-binding protein in brain and the only
serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM),
which plays a critical role in coupling Ca2+ signals to cellular responses. CaM
up-regulates the phosphatase activity of calcineurin by binding to the
CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal
structural studies of CaM bound to a CBD peptide. The chimeric protein
containing CaM and the CBD peptide forms an intimate homodimer, in which CaM
displays a native-like extended conformation and the CBD peptide shows
alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the
C-terminal lobe from the second molecule form a combined binding site to trap
the peptide. Thus, the dimer provides two binding sites, each of which is
reminiscent of the fully collapsed conformation of CaM commonly observed in
complex with, for example, the myosin light chain kinase (MLCK) peptide. The
interaction between the peptide and CaM is highly specific and similar to MLCK.
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