1tnq: Difference between revisions

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[[Image:1tnq.jpg|left|200px]]<br /><applet load="1tnq" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1tnq.jpg|left|200px]]<br /><applet load="1tnq" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1tnq" />

'''STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH'''<br />

==Overview==

Regulation of contraction in skeletal muscle occurs through calcium, binding to the protein troponin C. The solution structures of the, regulatory domain of apo and calcium-loaded troponin C have been, determined by multinuclear, multidimensional nuclear magnetic resonance, techniques. The structural transition in the regulatory domain of troponin, C on calcium binding involves an opening of the structure through large, changes in interhelical angles. This leads to the increased exposure of an, extensive hydrophobic patch, an event that triggers skeletal muscle, contraction.

Regulation of contraction in skeletal muscle occurs through calcium binding to the protein troponin C. The solution structures of the regulatory domain of apo and calcium-loaded troponin C have been determined by multinuclear, multidimensional nuclear magnetic resonance techniques. The structural transition in the regulatory domain of troponin C on calcium binding involves an opening of the structure through large changes in interhelical angles. This leads to the increased exposure of an extensive hydrophobic patch, an event that triggers skeletal muscle contraction.

==About this Structure==

1TNQ 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=1TNQ OCA].

1TNQ 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=1TNQ OCA].

==Reference==

Line 13:

[[Category: Gallus gallus]]

[[Category: Single protein]]

[[Category: Gagne, S.M.]]

[[Category: Gagne, S M.]]

[[Category: Sykes, B.D.]]

[[Category: Sykes, B D.]]

[[Category: CA]]

[[Category: ef-hand]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 03:26:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:30 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tnq.jpg|left|200px]]<br /><applet load="1tnq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tnq.jpg|left|200px]]<br /><applet load="1tnq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tnq" />
 '''STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH'''<br />
 ==Overview==
-Regulation of contraction in skeletal muscle occurs through calcium, binding to the protein troponin C. The solution structures of the, regulatory domain of apo and calcium-loaded troponin C have been, determined by multinuclear, multidimensional nuclear magnetic resonance, techniques. The structural transition in the regulatory domain of troponin, C on calcium binding involves an opening of the structure through large, changes in interhelical angles. This leads to the increased exposure of an, extensive hydrophobic patch, an event that triggers skeletal muscle, contraction.
+Regulation of contraction in skeletal muscle occurs through calcium binding to the protein troponin C. The solution structures of the regulatory domain of apo and calcium-loaded troponin C have been determined by multinuclear, multidimensional nuclear magnetic resonance techniques. The structural transition in the regulatory domain of troponin C on calcium binding involves an opening of the structure through large changes in interhelical angles. This leads to the increased exposure of an extensive hydrophobic patch, an event that triggers skeletal muscle contraction.
 ==About this Structure==
-TNQ 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=1TNQ OCA].
+TNQ 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=1TNQ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
-[[Category: Gagne, S.M.]]
+[[Category: Gagne, S M.]]
-[[Category: Sykes, B.D.]]
+[[Category: Sykes, B D.]]
 [[Category: CA]]
 [[Category: ef-hand]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:26:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:30 2008''