Structural comparison of the active site channels in rodent and primate vascular adhesion protein-1

Eva Bligt-Lindén, R Arunachalam, Vimal Parkash, Tiina Salminen

Research output: Contribution to journalArticleScientificpeer-review

6 Citations (Scopus)

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 alpha-helix of the D3 domain together with C-terminal residues are likely to affect ligand recognition and binding.
Original languageUndefined/Unknown
Pages (from-to)947–950
Number of pages4
JournalJournal of Neural Transmission
Volume120
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Keywords

  • AOC3
  • Human VAP-1
  • Rodent VAP-1
  • Structural comparison
  • Ligand recognition

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