3CYS: DETERMINATION OF THE NMR SOLUTION STRUCTURE OF THE CYCLOPHILIN A-CYCLOSPORIN A COMPLEX

Citation:
Abstract
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.
PDB ID: 3CYSDownload
MMDB ID: 74832
PDB Deposition Date: 1994/2/28
Updated in MMDB: 2017/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 3CYS: dimeric; determined by software (PISA)
Molecular Components in 3CYS
Label Count Molecule
Protein (1 molecule)
1
Peptidyl-prolyl Cis-trans Isomerase a
Molecule annotation
Nucleotide(1 molecule)
1
Cyclosporin a
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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