1cmg: Difference between revisions

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[[Image:1cmg.~~gif~~|left|200px]]

[[Image:1cmg.png|left|200px]]

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~~'''~~NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN~~'''~~

===NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_7552749}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7552749 is the PubMed ID number.

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==About this Structure==

1CMG is a [[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=1CMG OCA].

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

==Reference==

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[[Category: Waltho, J P.]]

[[Category: Calcium-binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:53:33 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:56:55 2008''

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-[[Image:1cmg.gif|left|200px]]
+{{Seed}}
+[[Image:1cmg.png|left|200px]]
 <!--
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 {{STRUCTURE_1cmg|  PDB=1cmg  |  SCENE=  }}
-'''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN'''
+===NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7552749}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7552749 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7552749}}
 ==About this Structure==
-CMG is a [[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=1CMG OCA].
+CMG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMG OCA].
 ==Reference==
@@ Line 29: / Line 33: @@
 [[Category: Waltho, J P.]]
 [[Category: Calcium-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:53:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:56:55 2008''