1cmf: Difference between revisions

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

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

caption="1cmf" />

'''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br />

==Overview==

We have determined the solution structures of the apo and (Ca2+)2 forms of, the carboxy-terminal domain of calmodulin using multidimensional, heteronuclear nuclear magnetic resonance spectroscopy. The results show, that both forms adopt well-defined structures with essentially equal, secondary structure. A comparison of the structures of the two forms shows, that Ca2+ binding causes major rearrangements of the secondary structure, elements with changes in inter-residue distances of up to 15 A and, exposure of the hydrophobic interior of the four-helix bundle. Comparisons, with previously determined high-resolution X-ray structures and models of, calmodulin indicate that this domain is structurally autonomous.

We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.

==About this Structure==

1CMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA].

1CMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA].

==Reference==

Line 15:

[[Category: Drakenberg, T.]]

[[Category: Evenas, J.]]

[[Category: Finn, B.E.]]

[[Category: Finn, B E.]]

[[Category: Forsen, S.]]

[[Category: Thulin, E.]]

[[Category: Waltho, J.P.]]

[[Category: Waltho, J P.]]

[[Category: calcium-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 12:34:~~50 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:30 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cmf.gif|left|200px]]<br /><applet load="1cmf" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cmf.gif|left|200px]]<br /><applet load="1cmf" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cmf" />
 '''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br />
 ==Overview==
-We have determined the solution structures of the apo and (Ca2+)2 forms of, the carboxy-terminal domain of calmodulin using multidimensional, heteronuclear nuclear magnetic resonance spectroscopy. The results show, that both forms adopt well-defined structures with essentially equal, secondary structure. A comparison of the structures of the two forms shows, that Ca2+ binding causes major rearrangements of the secondary structure, elements with changes in inter-residue distances of up to 15 A and, exposure of the hydrophobic interior of the four-helix bundle. Comparisons, with previously determined high-resolution X-ray structures and models of, calmodulin indicate that this domain is structurally autonomous.
+We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.
 ==About this Structure==
-CMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA].
+CMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Drakenberg, T.]]
 [[Category: Evenas, J.]]
-[[Category: Finn, B.E.]]
+[[Category: Finn, B E.]]
 [[Category: Forsen, S.]]
 [[Category: Thulin, E.]]
-[[Category: Waltho, J.P.]]
+[[Category: Waltho, J P.]]
 [[Category: calcium-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:34:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:30 2008''