3cys
From Proteopedia
(New page: 200px<br /><applet load="3cys" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cys" /> '''DETERMINATION OF THE NMR SOLUTION STRUCTURE ...) |
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'''DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX'''<br /> | '''DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional NMR solution structure of the cyclophilin A | + | The three-dimensional NMR solution structure of the cyclophilin A (Cyp)-cyclosporin A (CsA) complex was determined, and here we provide a detailed description of the analysis of the NMR data and the structure calculation. Using 15N- and 13C-resolved three- and four-dimensional [1H,1H]-nuclear Overhauser enhancement (NOE) spectroscopy with uniformly isotope-labeled Cyp in the complex, a final data set of 1810 intra-Cyp, 107 intra-CsA and 63 intermolecular NOE upper distance constraints was collected as input for the structure calculation with the program DIANA. A group of DIANA conformers, selected by a previously described analysis of the dependence of the maximal root-mean-square deviation (rmsd) among the individual conformers on the residual target function value, was subjected to energy refinement with the program FANTOM. The 22 best energy-refined conformers were then used to represent the solution structure. The average rmsd relative to the mean structure of these 22 conformers is 1.1 A for the backbone atoms of all residues of the complex. The molecular architecture of Cyp in the Cyp-CsA complex includes an eight-stranded antiparallel beta-barrel, which is closed on each side by an amphipathic helix. CsA is bound in a cavity formed by part of the barrel surface and four loops with nonregular secondary structure. Comparison of this structure with structures of Cyp-CsA and other Cyp-peptide complexes determined by different approaches shows extensive similarities. |
==About this Structure== | ==About this Structure== | ||
| - | 3CYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure | + | 3CYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure supersedes the now removed PDB entry 2CYS. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CYS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: isomerase(peptidyl-prolyl cis-trans)]] | [[Category: isomerase(peptidyl-prolyl cis-trans)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:59 2008'' |
Revision as of 17:09, 21 February 2008
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DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX
Overview
The three-dimensional NMR solution structure of the cyclophilin A (Cyp)-cyclosporin A (CsA) complex was determined, and here we provide a detailed description of the analysis of the NMR data and the structure calculation. Using 15N- and 13C-resolved three- and four-dimensional [1H,1H]-nuclear Overhauser enhancement (NOE) spectroscopy with uniformly isotope-labeled Cyp in the complex, a final data set of 1810 intra-Cyp, 107 intra-CsA and 63 intermolecular NOE upper distance constraints was collected as input for the structure calculation with the program DIANA. A group of DIANA conformers, selected by a previously described analysis of the dependence of the maximal root-mean-square deviation (rmsd) among the individual conformers on the residual target function value, was subjected to energy refinement with the program FANTOM. The 22 best energy-refined conformers were then used to represent the solution structure. The average rmsd relative to the mean structure of these 22 conformers is 1.1 A for the backbone atoms of all residues of the complex. The molecular architecture of Cyp in the Cyp-CsA complex includes an eight-stranded antiparallel beta-barrel, which is closed on each side by an amphipathic helix. CsA is bound in a cavity formed by part of the barrel surface and four loops with nonregular secondary structure. Comparison of this structure with structures of Cyp-CsA and other Cyp-peptide complexes determined by different approaches shows extensive similarities.
About this Structure
3CYS is a Single protein structure of sequence from [1]. This structure supersedes the now removed PDB entry 2CYS. Full crystallographic information is available from OCA.
Reference
Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex., Spitzfaden C, Braun W, Wider G, Widmer H, Wuthrich K, J Biomol NMR. 1994 Jul;4(4):463-82. PMID:8075536
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