1cmf
From Proteopedia
(New page: 200px<br /><applet load="1cmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmf" /> '''NMR SOLUTION STRUCTURE OF APO CALMODULIN CAR...) |
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| - | [[Image:1cmf.gif|left|200px]]<br /><applet load="1cmf" size=" | + | [[Image:1cmf.gif|left|200px]]<br /><applet load="1cmf" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br /> | '''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the solution structures of the apo and (Ca2+)2 forms of | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Drakenberg, T.]] | [[Category: Drakenberg, T.]] | ||
[[Category: Evenas, J.]] | [[Category: Evenas, J.]] | ||
| - | [[Category: Finn, B | + | [[Category: Finn, B E.]] |
[[Category: Forsen, S.]] | [[Category: Forsen, S.]] | ||
[[Category: Thulin, E.]] | [[Category: Thulin, E.]] | ||
| - | [[Category: Waltho, J | + | [[Category: Waltho, J P.]] |
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:30 2008'' |
Revision as of 10:07, 21 February 2008
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NMR SOLUTION STRUCTURE OF APO 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.
About this Structure
1CMF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Calcium-induced structural changes and domain autonomy in calmodulin., Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsen S, Nat Struct Biol. 1995 Sep;2(9):777-83. PMID:7552749
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