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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
- Source :
- Protein Engineering Design and Selection. 11:1195-1204
- Publication Year :
- 1998
- Publisher :
- Oxford University Press (OUP), 1998.
-
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 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.
- Subjects :
- Models, Molecular
Amine oxidase
Glycosylation
Protein Conformation
Monoamine oxidase
Molecular Sequence Data
Bioengineering
Biochemistry
chemistry.chemical_compound
Cell Adhesion
Humans
Amino Acid Sequence
Disulfides
Cell adhesion
Molecular Biology
chemistry.chemical_classification
Oxidoreductases Acting on CH-NH Group Donors
Binding Sites
Molecular Structure
biology
Chemistry
Cell adhesion molecule
Active site
Adhesion
biology.protein
Amine Oxidase (Copper-Containing)
Glycoprotein
Cell Adhesion Molecules
Dimerization
Oligopeptides
Sequence Alignment
Copper
Biotechnology
Subjects
Details
- ISSN :
- 17410134 and 17410126
- Volume :
- 11
- Database :
- OpenAIRE
- Journal :
- Protein Engineering Design and Selection
- Accession number :
- edsair.doi.dedup.....157da9a6458d1d00707a2816648beeba