1j1d: Difference between revisions
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|PDB= 1j1d |SIZE=350|CAPTION= <scene name='initialview01'>1j1d</scene>, resolution 2.61Å | |PDB= 1j1d |SIZE=350|CAPTION= <scene name='initialview01'>1j1d</scene>, resolution 2.61Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1j1e|1J1E]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1d OCA], [http://www.ebi.ac.uk/pdbsum/1j1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j1d RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Troponin is essential in Ca(2+) regulation of skeletal and cardiac muscle contraction. It consists of three subunits (TnT, TnC and TnI) and, together with tropomyosin, is located on the actin filament. Here we present crystal structures of the core domains (relative molecular mass of 46,000 and 52,000) of human cardiac troponin in the Ca(2+)-saturated form. Analysis of the four-molecule structures reveals that the core domain is further divided into structurally distinct subdomains that are connected by flexible linkers, making the entire molecule highly flexible. The alpha-helical coiled-coil formed between TnT and TnI is integrated in a rigid and asymmetric structure (about 80 angstrom long), the IT arm, which bridges putative tropomyosin-anchoring regions. The structures of the troponin ternary complex imply that Ca(2+) binding to the regulatory site of TnC removes the carboxy-terminal portion of TnI from actin, thereby altering the mobility and/or flexibility of troponin and tropomyosin on the actin filament. | Troponin is essential in Ca(2+) regulation of skeletal and cardiac muscle contraction. It consists of three subunits (TnT, TnC and TnI) and, together with tropomyosin, is located on the actin filament. Here we present crystal structures of the core domains (relative molecular mass of 46,000 and 52,000) of human cardiac troponin in the Ca(2+)-saturated form. Analysis of the four-molecule structures reveals that the core domain is further divided into structurally distinct subdomains that are connected by flexible linkers, making the entire molecule highly flexible. The alpha-helical coiled-coil formed between TnT and TnI is integrated in a rigid and asymmetric structure (about 80 angstrom long), the IT arm, which bridges putative tropomyosin-anchoring regions. The structures of the troponin ternary complex imply that Ca(2+) binding to the regulatory site of TnC removes the carboxy-terminal portion of TnI from actin, thereby altering the mobility and/or flexibility of troponin and tropomyosin on the actin filament. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Takeda, S.]] | [[Category: Takeda, S.]] | ||
[[Category: Yamashita, A.]] | [[Category: Yamashita, A.]] | ||
[[Category: ca2+ binding protein]] | [[Category: ca2+ binding protein]] | ||
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
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[[Category: thin filament]] | [[Category: thin filament]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:32 2008'' | ||
Revision as of 21:27, 30 March 2008
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| , resolution 2.61Å | |||||||
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| Ligands: | |||||||
| Related: | 1J1E
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the 46kDa domain of human cardiac troponin in the Ca2+ saturated form
OverviewOverview
Troponin is essential in Ca(2+) regulation of skeletal and cardiac muscle contraction. It consists of three subunits (TnT, TnC and TnI) and, together with tropomyosin, is located on the actin filament. Here we present crystal structures of the core domains (relative molecular mass of 46,000 and 52,000) of human cardiac troponin in the Ca(2+)-saturated form. Analysis of the four-molecule structures reveals that the core domain is further divided into structurally distinct subdomains that are connected by flexible linkers, making the entire molecule highly flexible. The alpha-helical coiled-coil formed between TnT and TnI is integrated in a rigid and asymmetric structure (about 80 angstrom long), the IT arm, which bridges putative tropomyosin-anchoring regions. The structures of the troponin ternary complex imply that Ca(2+) binding to the regulatory site of TnC removes the carboxy-terminal portion of TnI from actin, thereby altering the mobility and/or flexibility of troponin and tropomyosin on the actin filament.
About this StructureAbout this Structure
1J1D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form., Takeda S, Yamashita A, Maeda K, Maeda Y, Nature. 2003 Jul 3;424(6944):35-41. PMID:12840750
Page seeded by OCA on Sun Mar 30 21:27:32 2008