3cys: Difference between revisions
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|PDB= 3cys |SIZE=350|CAPTION= <scene name='initialview01'>3cys</scene> | |PDB= 3cys |SIZE=350|CAPTION= <scene name='initialview01'>3cys</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cys OCA], [http://www.ebi.ac.uk/pdbsum/3cys PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3cys RCSB]</span> | |||
}} | }} | ||
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[[Category: isomerase(peptidyl-prolyl cis-trans)]] | [[Category: isomerase(peptidyl-prolyl cis-trans)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:52 2008'' | ||
Revision as of 02:32, 31 March 2008
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| 3cys | |||||||||||||
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| Ligands: | ABA, BMT, MLE, MVA, SAR | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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