1scv: Difference between revisions

Revision as of 01:46, 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:1scv.png

Template:STRUCTURE 1scv

NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN INMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I

Template:ABSTRACT PUBMED 15350124

About this StructureAbout this Structure

1SCV is a Single protein structure of sequence from Gallus gallus. Full experimental information is available from OCA.

ReferenceReference

Structure of the Mg2+-loaded C-lobe of cardiac troponin C bound to the N-domain of cardiac troponin I: comparison with the Ca2+-loaded structure., Finley NL, Howarth JW, Rosevear PR, Biochemistry. 2004 Sep 14;43(36):11371-9. PMID:15350124

Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I., Gasmi-Seabrook GM, Howarth JW, Finley N, Abusamhadneh E, Gaponenko V, Brito RM, Solaro RJ, Rosevear PR, Biochemistry. 1999 Jun 29;38(26):8313-22. PMID:10387077

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OCA

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 {{STRUCTURE_1scv|  PDB=1scv  |  SCENE=  }}
-'''NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I'''
+===NMR STRUCTURE OF THE C TERMINAL DOMAIN OF CARDIAC TROPONIN C BOUND TO THE N TERMINAL DOMAIN OF CARDIAC TROPONIN I===
-==Overview==
+<!--
-Cardiac troponin C (cTnC) is the Ca(2+)-binding component of the troponin complex and, as such, is the Ca(2+)-dependent switch in muscle contraction. This protein consists of two globular lobes, each containing a pair of EF-hand metal-binding sites, connected by a linker. In the N lobe, Ca(2+)-binding site I is inactive and Ca(2+)-binding site II is primarily responsible for initiation of muscle contraction. The C lobe contains Ca(2+)/Mg(2+)-binding sites III and IV, which bind Mg(2+) with lower affinity and play a structural as well as a secondary role in modulating the Ca(2+) signal. To understand the structural consequences of Ca(2+)/Mg(2+) exchange in the C lobe, we have determined the NMR solution structure of the Mg(2+)-loaded C lobe, cTnC(81-161), in a complex with the N domain of cardiac troponin I, cTnI(33-80), and compared it with a refined Ca(2+)-loaded structure. The overall tertiary structure of the Mg(2+)-loaded C lobe is very similar to that of the refined Ca(2+)-loaded structure as evidenced by the root-mean-square deviation of 0.94 A for all backbone atoms. While metal-dependent conformational changes are minimal, substitution of Mg(2+) for Ca(2+) is characterized by condensation of the C-terminal portion of the metal-binding loops with monodentate Mg(2+) ligation by the conserved Glu at position 12 and partial closure of the cTnI hydrophobic binding cleft around site IV. Thus, conformational plasticity in the Ca(2+)/Mg(2+)-dependent binding loops may represent a mechanism to modulate C-lobe cTnC interactions with the N domain of cTnI.
+The line below this paragraph, {{ABSTRACT_PUBMED_15350124}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15350124 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15350124}}
 ==About this Structure==
-SCV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCV OCA].
+SCV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCV OCA].
 ==Reference==
 Structure of the Mg2+-loaded C-lobe of cardiac troponin C bound to the N-domain of cardiac troponin I: comparison with the Ca2+-loaded structure., Finley NL, Howarth JW, Rosevear PR, Biochemistry. 2004 Sep 14;43(36):11371-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15350124 15350124]
+Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I., Gasmi-Seabrook GM, Howarth JW, Finley N, Abusamhadneh E, Gaponenko V, Brito RM, Solaro RJ, Rosevear PR, Biochemistry. 1999 Jun 29;38(26):8313-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10387077 10387077]
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
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 [[Category: Muscle protein]]
 [[Category: Troponin c-troponin i interaction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:33:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:45:56 2008''