1aj4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1aj4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj4" /> '''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPO...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1aj4.gif|left|200px]]<br /><applet load="1aj4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1aj4.gif|left|200px]]<br /><applet load="1aj4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1aj4" />
caption="1aj4" />
'''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 1 STRUCTURE'''<br />
'''STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 1 STRUCTURE'''<br />


==Overview==
==Overview==
The regulation of cardiac muscle contraction must differ from that of, skeletal muscles to effect different physiological and contractile, properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle, contraction, possesses different functional and Ca2+-binding properties, compared with skeletal TnC and features a Ca2+-binding site I, which is, naturally inactive. The structure of cardiac TnC in the Ca2+-saturated, state has been determined by nuclear magnetic resonance spectroscopy. The, regulatory domain exists in a "closed" conformation even in the Ca2+-bound, (the "on") state, in contrast to all predicted models and differing, significantly from the calcium-induced structure observed in skeletal TnC., This structure in the Ca2+-bound state, and its subsequent interaction, with troponin I (TnI), are crucial in determining the specific regulatory, mechanism for cardiac muscle contraction. Further, it will allow for an, understanding of the action of calcium-sensitizing drugs, which bind to, cardiac TnC and are known to enhance the ability of cardiac TnC to, activate cardiac muscle contraction.
The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.


==About this Structure==
==About this Structure==
1AJ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AJ4 OCA].  
1AJ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ4 OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gagne, S.M.]]
[[Category: Gagne, S M.]]
[[Category: Li, M.X.]]
[[Category: Li, M X.]]
[[Category: Liu, W.]]
[[Category: Liu, W.]]
[[Category: Putkey, J.A.]]
[[Category: Putkey, J A.]]
[[Category: Sia, S.K.]]
[[Category: Sia, S K.]]
[[Category: Spyracopoulos, L.]]
[[Category: Spyracopoulos, L.]]
[[Category: Sykes, B.D.]]
[[Category: Sykes, B D.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium binding]]
[[Category: calcium binding]]
Line 26: Line 26:
[[Category: regulatory]]
[[Category: regulatory]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:53:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:05 2008''

Revision as of 09:45, 21 February 2008

File:1aj4.gif


1aj4

Drag the structure with the mouse to rotate

STRUCTURE OF CALCIUM-SATURATED CARDIAC TROPONIN C, NMR, 1 STRUCTURE

Overview

The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.

About this Structure

1AJ4 is a Single protein structure of sequence from Gallus gallus with CA as ligand. Full crystallographic information is available from OCA.

Reference

Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain., Sia SK, Li MX, Spyracopoulos L, Gagne SM, Liu W, Putkey JA, Sykes BD, J Biol Chem. 1997 Jul 18;272(29):18216-21. PMID:9218458

Page seeded by OCA on Thu Feb 21 11:45:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA