2ix7: Difference between revisions
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|PDB= 2ix7 |SIZE=350|CAPTION= <scene name='initialview01'>2ix7</scene>, resolution 2.50Å | |PDB= 2ix7 |SIZE=350|CAPTION= <scene name='initialview01'>2ix7</scene>, resolution 2.50Å | ||
|SITE= <scene name='pdbsite=AC1:CYS+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:CYS+Binding+Site+For+Chain+C'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ix7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix7 OCA], [http://www.ebi.ac.uk/pdbsum/2ix7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ix7 RCSB]</span> | |||
}} | }} | ||
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[[Category: Mui, S.]] | [[Category: Mui, S.]] | ||
[[Category: Trybus, K M.]] | [[Category: Trybus, K M.]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:56 2008'' | ||
Revision as of 00:49, 31 March 2008
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| 2ix7, resolution 2.50Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CYS, SO4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V
Overview
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 Structure
2IX7 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 03:49:56 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Mus musculus
- Protein complex
- Cohen, C.
- Gaucher, J F.
- Houdusse, A.
- Krementsova, E.
- Mui, S.
- Trybus, K M.
- 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
