1yv0: Difference between revisions

Revision as of 01:17, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1yv0.png

Template:STRUCTURE 1yv0

Crystal structure of skeletal muscle troponin in the Ca2+-free stateCrystal structure of skeletal muscle troponin in the Ca2+-free state

Template:ABSTRACT PUBMED 15784741

About this StructureAbout this Structure

1YV0 is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Ca(2+)-regulated structural changes in troponin., Vinogradova MV, Stone DB, Malanina GG, Karatzaferi C, Cooke R, Mendelson RA, Fletterick RJ, Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5038-43. Epub 2005 Mar 22. PMID:15784741

Page seeded by OCA on Mon Jul 28 01:17:19 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of skeletal muscle troponin in the Ca2+-free state'''
+===Crystal structure of skeletal muscle troponin in the Ca2+-free state===
-==Overview==
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-Troponin senses Ca2+ to regulate contraction in striated muscle. Structures of skeletal muscle troponin composed of TnC (the sensor), TnI (the regulator), and TnT (the link to the muscle thin filament) have been determined. The structure of troponin in the Ca(2+)-activated state features a nearly twofold symmetrical assembly of TnI and TnT subunits penetrated asymmetrically by the dumbbell-shaped TnC subunit. Ca ions are thought to regulate contraction by controlling the presentation to and withdrawal of the TnI inhibitory segment from the thin filament. Here, we show that the rigid central helix of the sensor binds the inhibitory segment of TnI in the Ca(2+)-activated state. Comparison of crystal structures of troponin in the Ca(2+)-activated state at 3.0 angstroms resolution and in the Ca(2+)-free state at 7.0 angstroms resolution shows that the long framework helices of TnI and TnT, presumed to be a Ca(2+)-independent structural domain of troponin are unchanged. Loss of Ca ions causes the rigid central helix of the sensor to collapse and to release the inhibitory segment of TnI. The inhibitory segment of TnI changes conformation from an extended loop in the presence of Ca2+ to a short alpha-helix in its absence. We also show that Anapoe, a detergent molecule, increases the contractile force of muscle fibers and binds specifically, together with the TnI switch helix, in a hydrophobic pocket of TnC upon activation by Ca ions.
+The line below this paragraph, {{ABSTRACT_PUBMED_15784741}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15784741 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15784741}}
 ==About this Structure==
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 [[Category: Thin filament]]
 [[Category: Troponin]]
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