3bas: Difference between revisions

Revision as of 19:10, 27 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:3bas.png

Template:STRUCTURE 3bas

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) formCrystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form

Template:ABSTRACT PUBMED 18155233

About this StructureAbout this Structure

3BAS is a Single protein structure of sequence from Argopecten irradians, saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins., Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C, J Mol Biol. 2008 Feb 1;375(5):1434-43. Epub 2007 Nov 28. PMID:18155233

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

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

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

OCA

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-'''Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form'''
+===Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form===
-==Overview==
+<!--
-The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the two heads of this dimeric molecule and is key to its function. Previously, a crystal structure of this predominantly coiled-coil region was determined for a short fragment (51 residues plus a leucine zipper) of the scallop striated muscle myosin isoform. In that study, the N-terminal 10-14 residues were found to be disordered. We have now determined the structure of the same scallop peptide in three additional crystal environments. In each of two of these structures, improved order has allowed visualization of the entire N-terminus in one chain of the dimeric peptide. We have also compared the melting temperatures of this scallop S2 peptide with those of analogous peptides from three other isoforms. Taken together, these experiments, along with examination of sequences, point to a diminished stability of the N-terminal region of S2 in regulated myosins, compared with those myosins whose regulation is thin filament linked. It seems plain that this isoform-specific instability promotes the off-state conformation of the heads in regulated myosins. We also discuss how myosin isoforms with varied thermal stabilities share the basic capacity to transmit force efficiently in order to produce contraction in their on states.
+The line below this paragraph, {{ABSTRACT_PUBMED_18155233}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18155233 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18155233}}
 ==About this Structure==
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 ==Reference==
 An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins., Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C, J Mol Biol. 2008 Feb 1;375(5):1434-43. Epub 2007 Nov 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18155233 18155233]
+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]
+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]
 [[Category: Argopecten irradians, saccharomyces cerevisiae]]
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 [[Category: Salt link]]
 [[Category: Thick filament]]
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