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

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Salminen TA, Smith DJ, Jalkanen S, Johnson MS
Publisher: OXFORD UNIV PRESS
Publication year: 1998
Journal: Protein Engineering, Design and Selection
Journal acronym: PROTEIN ENG
Volume number: 11
Issue number: 12
Start page: 1195
End page: 1204
Number of pages: 10
ISSN: 0269-2139
eISSN: 1741-0134


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.


Keywords

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

Last updated on 2019-13-11 at 03:10