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2fxm

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[[Image:2fxm.gif|left|200px]]
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{{STRUCTURE_2fxm| PDB=2fxm | SCENE= }}
{{STRUCTURE_2fxm| PDB=2fxm | SCENE= }}
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'''Structure of the human beta-myosin S2 fragment'''
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===Structure of the human beta-myosin S2 fragment===
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==Overview==
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Myosin II is the major component of the muscle thick filament. It consists of two N-terminal S1 subfragments ("heads") connected to a long dimeric coiled-coil rod. The rod is in itself twofold symmetric, but in the filament, the two heads point away from the filament surface and are therefore not equivalent. This breaking of symmetry requires the initial section of the rod, subfragment 2 (S2), to be relatively flexible. S2 is an important functional element, involved in various mechanisms by which the activity of smooth and striated muscle is regulated. We have determined crystal structures of the 126 N-terminal residues of S2 from human cardiac beta-myosin II (S2-Delta), of both WT and the disease-associated E924K mutant. S2-Delta is a straight parallel dimeric coiled coil, but the N terminus of one chain is disordered in WT-S2-Delta due to crystal contacts, indicative of unstable local structure. Bulky noncanonical side chains pack into a/d positions of S2-Delta's N terminus, leading to defined local asymmetry and axial stagger, which could induce nonequivalence of the S1 subfragments. Additionally, S2 possesses a conserved charge distribution with three prominent rings of negative potential within S2-Delta, the first of which may provide a binding interface for the "blocked head" of smooth muscle myosin in the OFF state. The observation that many disease-associated mutations affect the second negatively charged ring further suggests that charge interactions play an important role in regulation of cardiac muscle activity through myosin-binding protein C.
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(as it appears on PubMed at http://www.pubmed.gov), where 17095604 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17095604}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment., Blankenfeldt W, Thoma NH, Wray JS, Gautel M, Schlichting I, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17713-7. Epub 2006 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17095604 17095604]
Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment., Blankenfeldt W, Thoma NH, Wray JS, Gautel M, Schlichting I, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17713-7. Epub 2006 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17095604 17095604]
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Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C., Gruen M, Gautel M, J Mol Biol. 1999 Feb 26;286(3):933-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10024460 10024460]
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Visualization of an unstable coiled coil from the scallop myosin rod., Li Y, Brown JH, Reshetnikova L, Blazsek A, Farkas L, Nyitray L, Cohen C, Nature. 2003 Jul 17;424(6946):341-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12867988 12867988]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Familial hypertrophic cardiomyopathy]]
[[Category: Familial hypertrophic cardiomyopathy]]
[[Category: Thick filament]]
[[Category: Thick filament]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:25:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:15:54 2008''

Revision as of 01:15, 28 July 2008

Image:2fxm.png

Template:STRUCTURE 2fxm

Structure of the human beta-myosin S2 fragment

Template:ABSTRACT PUBMED 17095604

About this Structure

2FXM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment., Blankenfeldt W, Thoma NH, Wray JS, Gautel M, Schlichting I, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17713-7. Epub 2006 Nov 9. PMID:17095604

Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C., Gruen M, Gautel M, J Mol Biol. 1999 Feb 26;286(3):933-49. PMID:10024460

Visualization of an unstable coiled coil from the scallop myosin rod., Li Y, Brown JH, Reshetnikova L, Blazsek A, Farkas L, Nyitray L, Cohen C, Nature. 2003 Jul 17;424(6946):341-5. PMID:12867988

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