1cmg: Difference between revisions
New page: left|200px<br /><applet load="1cmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmg" /> '''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CAL... |
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'''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br /> | '''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED 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== | ||
1CMG 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:// | 1CMG 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=1CMG 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 12:07:31 2008'' | ||
Revision as of 10:07, 21 February 2008
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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.
About this Structure
1CMG 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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