1us1: Difference between revisions
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[[Category: vascular adhesion protein-1]] | [[Category: vascular adhesion protein-1]] | ||
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Revision as of 17:04, 30 October 2007
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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 ... [(full description)]
About this StructureAbout this Structure
1US1 is a [Single protein] structure of sequence from [Homo sapiens] with NAG, CU and CA as [ligands]. Active as [Amine oxidase (copper-containing)], with EC number [1.4.3.6]. Structure known Active Site: AC1. 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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