Protein Engineering, Vol 11, 1195-1204, Copyright © 1998 by Oxford University Press
TA Salminen, DJ Smith, S Jalkanen and MS Johnson
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 D4, 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.
ARTICLES
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
Department of Biochemistry and Pharmacy, Abo Akademi University, Turku, Finland. tiina.salminen@btk.utu.fi
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