Structural model of the catalytic domain of an enzyme with cell adhesion activity: human vascular adhesion protein-1 (HVAP-1) D4 domain is an amine oxidase

Tiina Salminen, DJ Smith, S Jalkanen, Mark S Johnson

Research output: Contribution to journalArticleScientificpeer-review

43 Citations (Scopus)

Abstract

Human vascular adhesion protein-1 (HVAP-1) is a multifunctional protein having at least two different cellular roles, functioning both as a lymphocyte-endothelial cell adhesion protein and as an enzyme with monoamine oxidase activity. HVAP-1 is a 180 kDa homodimeric glycoprotein consisting of a membrane-spanning domain and three predicted extracellular copper-containing amine oxidase domains. In HVAP-1 the extracellular domains are composed of a large domain DJ, containing the active site and forming the interface of the dimer, while the smaller D2 and D3 domains surround the D4 dimer near the entrance to the active site. The structural model of the catalytic D4 domain of HVAP-1 reveals that all components necessary for enzymatic monoamine oxidase activity are indeed present within the HVAP-1 and pinpoints residues that may be key to substrate entry through a channel to the active site and residues likely to be involved in substrate specificity as well as structural features critical to dimer formation. Proper glycosylation is required for the cell adhesion function of HVAP-1 and the predicted location of the sugar units at the solvent-exposed surface suits this function well.
Original languageUndefined/Unknown
Pages (from-to)1195–1204
Number of pages10
JournalProtein Engineering, Design and Selection
Volume11
Issue number12
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

Keywords

  • activated structure
  • copper amine oxidase
  • structure and function
  • vascular adhesion protein-1 structure

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