期刊
JOURNAL OF APPLIED CRYSTALLOGRAPHY
卷 49, 期 -, 页码 158-167出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600576715022931
关键词
protein docking; polar Fourier correlation; point group symmetry; symmetry docking
资金
- Agence Nationale de la Recherche [ANR-11-MONU-006]
A novel fast Fourier transform-based ab inito docking algorithm called SAM is presented, for building perfectly symmetrical models of protein complexes with arbitrary point group symmetry. The basic approach uses a novel and very fast one-dimensional symmetry-constrained spherical polar Fourier search to assemble cyclic C-n systems from a given protein monomer. Structures with higher-order (D-n, T, O and I) point group symmetries may be built using a subsequent symmetry-constrained Fourier domain search to assemble trimeric sub-units. The results reported here show that the SAM algorithm can correctly assemble monomers of up to around 500 residues to produce a near-native complex structure with the given point group symmetry in 17 out of 18 test cases. The SAM program may be downloaded for academic use at http://sam.loria.fr/.
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