2jpw: Difference between revisions

Revision as of 21:22, 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:2jpw.png

Template:STRUCTURE 2jpw

Solution structure of the bisphosphorylated cardiac specific N-extension of cardiac troponin ISolution structure of the bisphosphorylated cardiac specific N-extension of cardiac troponin I

Template:ABSTRACT PUBMED 17854829

About this StructureAbout this Structure

2JPW is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin., Howarth JW, Meller J, Solaro RJ, Trewhella J, Rosevear PR, J Mol Biol. 2007 Oct 26;373(3):706-22. Epub 2007 Aug 22. PMID:17854829

Page seeded by OCA on Sun Jul 27 21:22:03 2008

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

OCA

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-[[Image:2jpw.jpg|left|200px]]
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 {{STRUCTURE_2jpw|  PDB=2jpw  |  SCENE=  }}
-'''Solution structure of the bisphosphorylated cardiac specific N-extension of cardiac troponin I'''
+===Solution structure of the bisphosphorylated cardiac specific N-extension of cardiac troponin I===
-==Overview==
+<!--
-We present here the solution structure for the bisphosphorylated form of the cardiac N-extension of troponin I (cTnI(1-32)), a region for which there are no previous high-resolution data. Using this structure, the X-ray crystal structure of the cardiac troponin core, and uniform density models of the troponin components derived from neutron contrast variation data, we built atomic models for troponin that show the conformational transition in cardiac troponin induced by bisphosphorylation. In the absence of phosphorylation, our NMR data and sequence analyses indicate a less structured cardiac N-extension with a propensity for a helical region surrounding the phosphorylation motif, followed by a helical C-terminal region (residues 25-30). In this conformation, TnI(1-32) interacts with the N-lobe of cardiac troponin C (cTnC) and thus is positioned to modulate myofilament Ca2+-sensitivity. Bisphosphorylation at Ser23/24 extends the C-terminal helix (residues 21-30) which results in weakening interactions with the N-lobe of cTnC and a re-positioning of the acidic amino terminus of cTnI(1-32) for favorable interactions with basic regions, likely the inhibitory region of cTnI. An extended poly(L-proline)II helix between residues 11 and 19 serves as the rigid linker that aids in re-positioning the amino terminus of cTnI(1-32) upon bisphosphorylation at Ser23/24. We propose that it is these electrostatic interactions between the acidic amino terminus of cTnI(1-32) and the basic inhibitory region of troponin I that induces a bending of cTnI at the end that interacts with cTnC. This model provides a molecular mechanism for the observed changes in cross-bridge kinetics upon TnI phosphorylation.
+The line below this paragraph, {{ABSTRACT_PUBMED_17854829}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17854829 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17854829}}
 ==About this Structure==
-JPW is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPW OCA].
+JPW is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPW OCA].
 ==Reference==
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 [[Category: Trewhella, J.]]
 [[Category: Contractile protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:10:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:22:03 2008''