title: TRAF2 docking with related proteins in silico studies.
abstract: Using the protein-protein docking program,           this study investigates the relationship between           TRAF2 and its related proteins and the diversity           within the 3D structures of TRAF2s. TRAF2           exists in monomer, trimer, and hexamer forms and it           can combine with a number of proteins. Through           comparative analysis we found that TRAF2(122),           TRAF2(22), TRAF2(21740), TRAF2(2), TRAF2(           22ABC), and TRAF2(Phyre) perform very close homoousia           in docking with the same group of ligands,           though these TRAF2s come from different sources.           The TRAF2-related proteins of cluster 1 change docking           values strongly from top to bottom. The TRAF2-           related proteins of clusters 2 and 3 have acceptable           variation of the docking values. In consideration of           the amino acid percentage, TRAF2-related proteins of           cluster 2 represent appropriate docking values.
authors.affiliation: Department of Medical Biology, Hubei University of Medicine, Hubei, PRC. zengfanlong0@163.com
authors.forename: F
authors.initials: F
authors.lastname: Zeng
authors.forename: Q
authors.initials: Q
authors.lastname: Wu
authors.forename: E
authors.initials: E
authors.lastname: Guo
authors.forename: H
authors.initials: H
authors.lastname: Guo
authors.forename: H
authors.initials: H
authors.lastname: Wang
authors.forename: J
authors.initials: J
authors.lastname: Shan
authors.forename: R
authors.initials: R
authors.lastname: Wei
mesh_terms: D000596:Amino Acids; D016000:Cluster Analysis; D019295:Computational Biology / Q000379:methods*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D047992:TNF Receptor-Associated Factor 2 / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D008024:Ligands; D047992:TNF Receptor-Associated Factor 2