1us1
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CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1
OverviewOverview
The expression of human vascular adhesion protein-1 (hVAP-1) is induced at, sites of inflammation where extravasation of lymphocytes from blood to the, peripheral tissue occurs. We have solved the X-ray structure of hVAP-1, a, human copper amine oxidase (CAO), which is distinguished from other CAOs, in being membrane-bound. The dimer structure reveals some intriguing, features that may have fundamental roles in the adhesive and enzymatic, functions of hVAP-1, especially regarding the role of hVAP-1 in, inflammation, lymphocyte attachment, and signaling. Firstly, Leu469 at the, substrate channel may play a key role in controlling the substrate entry;, depending on its conformation, it either blocks or gives access to the, active site. Secondly, sugar units are clearly observed at two of the six, predicted N-glycosylation sites. Moreover, mutagenesis analysis showed, that all of the predicted sites were glycosylated in the protein used for, crystallization. Thirdly, the existence of a solvent-exposed RGD motif at, the entrance to each active site in hVAP-1 suggests that it may have a, functional role.
About this StructureAbout this Structure
1US1 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications., Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA, Protein Sci. 2005 Aug;14(8):1964-74. PMID:16046623
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