title: Structural comparison of the active site channels in rodent and primate vascular adhesion protein-1.
abstract: In this study, we have made homology models of mouse, rat, and monkey vascular adhesion protein-1 (VAP-1) to reveal basis for the species-specific ligand recognition of VAP-1. Based on the structural comparisons, rodent VAP-1s have a narrower active site channel than primate VAP-1s. The variable residues in mouse and rat VAP-1, Phe447 from arm I and the polar residues from the first α-helix of the D3 domain together with C-terminal residues are likely to affect ligand recognition and binding.
authors: Structural Bioinformatics Laboratory, Department of Biosciences, Åbo Akademi University, Tykistökatu 6A, 20520, Turku, Finland.
authors: Eva
authors: E
authors: Bligt-Lindén
authors: Ramaiah
authors: R
authors: Arunachalam
authors: Vimal
authors: V
authors: Parkash
authors: Tiina Annamaria
authors: TA
authors: Salminen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000187:drug effects / Q000502:physiology; D005075:Biological Evolution; D020134:Catalytic Domain / Q000187:drug effects / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism*; D003198:Computer Simulation; D000882:Haplorhini; D006801:Humans; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D051381:Rats
chemical_list: D015815:Cell Adhesion Molecules; D008024:Ligands