期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 7, 页码 4535-4538出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C000857200
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资金
- NHLBI NIH HHS [HL26043] Funding Source: Medline
- NIDDK NIH HHS [DK44322] Funding Source: Medline
- NIGMS NIH HHS [GM40528] Funding Source: Medline
A novel translocation step is inferred from structural studies of the interactions between the intracellular calcium receptor protein calmodulin (CaM) and one of its regulatory targets. A mutant of CaM missing residues 2-8 (Delta NCaM) binds skeletal muscle myosin light chain kinase with high affinity but fails to activate catalysis. Small angle x-ray scattering data reveal that Delta NCaM occupies a position near the catalytic cleft in its complex with the kinase, whereas the native protein translocates to a position near the C-terminal end of the catalytic core. Thus, CaM residues 2-8 appear to facilitate movement of bound CaM away from the vicinity of the catalytic cleft.
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