1dmo: Difference between revisions

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

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

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~~'''~~CALMODULIN, NMR, 30 STRUCTURES~~'''~~

===CALMODULIN, NMR, 30 STRUCTURES===

~~==Overview==~~

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The ~~solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy~~, ~~and is compared~~ to the ~~previously reported structure of the Ca~~(~~2+)-saturated form~~. ~~The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees~~. ~~This leads to major changes in surface properties~~, ~~including the closure of~~ the ~~deep hydrophobic cavity essential for target protein recognition~~. ~~Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)~~-~~binding property observed between two adjacent EF~~-~~hand sites in the amino- and carboxy-terminal domains.~~

The line below this paragraph, {{ABSTRACT_PUBMED_7552747}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7552747 is the PubMed ID number.

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==About this Structure==

1DMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA].

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

==Reference==

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[[Category: Calcium-binding protein]]

[[Category: Calcium-induced conformational change]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 14~~:01:49 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:18:22 2008''

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-[[Image:1dmo.gif|left|200px]]
+{{Seed}}
+[[Image:1dmo.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dmo|  PDB=1dmo  |  SCENE=  }}
-'''CALMODULIN, NMR, 30 STRUCTURES'''
+===CALMODULIN, NMR, 30 STRUCTURES===
-==Overview==
+<!--
-The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.
+The line below this paragraph, {{ABSTRACT_PUBMED_7552747}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7552747 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7552747}}
 ==About this Structure==
-DMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA].
+DMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA].
 ==Reference==
@@ Line 27: / Line 31: @@
 [[Category: Calcium-binding protein]]
 [[Category: Calcium-induced conformational change]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:01:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:18:22 2008''