1kqv
From Proteopedia
(New page: 200px<br /><applet load="1kqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kqv" /> '''Family of NMR Solution Structures of Ca Ln C...) |
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| - | [[Image:1kqv.gif|left|200px]]<br /><applet load="1kqv" size=" | + | [[Image:1kqv.gif|left|200px]]<br /><applet load="1kqv" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Family of NMR Solution Structures of Ca Ln Calbindin D9K'''<br /> | '''Family of NMR Solution Structures of Ca Ln Calbindin D9K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The relative importance of paramagnetism-based constraints (i.e. | + | The relative importance of paramagnetism-based constraints (i.e. pseudocontact shifts, residual dipolar couplings and nuclear relaxation enhancements) with respect to classical constraints in solution structure determinations of paramagnetic metalloproteins has been addressed. The protein selected for the study is a calcium binding protein, calbindin D9k, in which one of the two calcium ions is substituted with cerium(III). From 1823 NOEs, 191 dihedral angles, 15 hydrogen bonds, 769 pseudocontact shifts, 64 orientational constraints, 26 longitudinal relaxation rates, plus 969 pseudocontact shifts from other lanthanides, a final family with backbone r.m.s.d. from the average of 0.25 A was obtained. Then, several families of structures were generated either by removing subsets of paramagnetism-based constraints or by removing increasing numbers of NOEs. The results show the relative importance of the various paramagnetism-based constraints and their good complementarity with the diamagnetic ones. Although a resolved structure cannot be obtained with paramagnetism-based constraints only, it is shown that a reasonably well resolved backbone fold can be safely obtained by retaining as few as 29 randomly chosen long-range NOEs using the standard version of the program PSEUDYANA. |
==About this Structure== | ==About this Structure== | ||
| - | 1KQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with LA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1KQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=LA:'>LA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: paramagnetism-based constraints]] | [[Category: paramagnetism-based constraints]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:58 2008'' |
Revision as of 11:37, 21 February 2008
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Family of NMR Solution Structures of Ca Ln Calbindin D9K
Overview
The relative importance of paramagnetism-based constraints (i.e. pseudocontact shifts, residual dipolar couplings and nuclear relaxation enhancements) with respect to classical constraints in solution structure determinations of paramagnetic metalloproteins has been addressed. The protein selected for the study is a calcium binding protein, calbindin D9k, in which one of the two calcium ions is substituted with cerium(III). From 1823 NOEs, 191 dihedral angles, 15 hydrogen bonds, 769 pseudocontact shifts, 64 orientational constraints, 26 longitudinal relaxation rates, plus 969 pseudocontact shifts from other lanthanides, a final family with backbone r.m.s.d. from the average of 0.25 A was obtained. Then, several families of structures were generated either by removing subsets of paramagnetism-based constraints or by removing increasing numbers of NOEs. The results show the relative importance of the various paramagnetism-based constraints and their good complementarity with the diamagnetic ones. Although a resolved structure cannot be obtained with paramagnetism-based constraints only, it is shown that a reasonably well resolved backbone fold can be safely obtained by retaining as few as 29 randomly chosen long-range NOEs using the standard version of the program PSEUDYANA.
About this Structure
1KQV is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.
Reference
Paramagnetism-based versus classical constraints: an analysis of the solution structure of Ca Ln calbindin D9k., Bertini I, Donaire A, Jimenez B, Luchinat C, Parigi G, Piccioli M, Poggi L, J Biomol NMR. 2001 Oct;21(2):85-98. PMID:11727989
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