Development of quantitative structure-binding affinity relationship models based on novel geometrical chemical descriptors of the protein-ligand interfaces.

ABSTRACT: Novel geometrical chemical descriptors have been derived on the basis of the computational geometry of protein-ligand interfaces and Pauling atomic electronegativities (EN). Delaunay tessellation has been applied to a diverse set of 517 X-ray characterized protein-ligand complexes yielding a unique collection of interfacial nearest neighbor atomic quadruplets for each complex. Each quadruplet composition was characterized by a single descriptor calculated as the sum of the EN values for the four participating atom types. We termed these simple descriptors generated from atomic EN values and derived with the Delaunay Tessellation the ENTess descriptors and used them in the variable selection k-nearest neighbor quantitative structure-binding affinity relationship (QSBR) studies of 264 divers

SUBMITTER: Zhang S 

PROVIDER: S-EPMC2773514 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature