Sammanfattning
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 alpha-helix of the D3 domain together with C-terminal residues are likely to affect ligand recognition and binding.
Originalspråk | Odefinierat/okänt |
---|---|
Sidor (från-till) | 947–950 |
Antal sidor | 4 |
Tidskrift | Journal of Neural Transmission |
Volym | 120 |
DOI | |
Status | Publicerad - 2013 |
MoE-publikationstyp | A1 Tidskriftsartikel-refererad |
Nyckelord
- AOC3
- Human VAP-1
- Rodent VAP-1
- Structural comparison
- Ligand recognition