2ix7
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STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V
OverviewOverview
A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the, first two IQ motifs of the murine myosin V heavy chain reveals an unusual, CaM conformation. The C-terminal lobe of each CaM adopts a semi-open, conformation that grips the first part of the IQ motif (IQxxxR), whereas, the N-terminal lobe adopts a closed conformation that interacts more, weakly with the second part of the motif (GxxxR). Variable residues in the, IQ motif play a critical role in determining the precise structure of the, bound CaM, such that even the consensus residues of different motifs show, unique interactions with CaM. This complex serves as a model for the lever, arm region of many classes of unconventional myosins, as well as other IQ, motif-containing proteins such as neuromodulin and IQGAPs.
About this StructureAbout this Structure
2IX7 is a [Protein complex] structure of sequences from [Mus musculus] with SO4 and CYS as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features., Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196
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- Mus musculus
- Protein complex
- Cohen, C.
- Gaucher, J.F.
- Houdusse, A.
- Krementsova, E.
- Mui, S.
- Trybus, K.M.
- CYS
- SO4
- Acetylation
- Actin-binding
- Atp-binding
- Ca2+ regulation
- Calcium
- Calmodulin
- Calmodulin-binding
- Coiled coil
- Complex
- Contractile protein
- Iq motif
- Metal binding
- Methylation
- Motor protein
- Myosin
- Nucleotide-binding
- Phosphorylation
- Ubl conjugation