1us1
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The expression of human vascular adhesion protein-1 (hVAP-1) is induced at | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Airenne, T | + | [[Category: Airenne, T T.]] |
| - | [[Category: Johnson, M | + | [[Category: Johnson, M S.]] |
[[Category: Kidron, H.]] | [[Category: Kidron, H.]] | ||
[[Category: Nymalm, Y.]] | [[Category: Nymalm, Y.]] | ||
| - | [[Category: Salminen, T | + | [[Category: Salminen, T A.]] |
[[Category: Soderholm, A.]] | [[Category: Soderholm, A.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: vascular adhesion protein-1]] | [[Category: vascular adhesion protein-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:38 2008'' |
Revision as of 13:27, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1
Overview
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 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.
Reference
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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