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| {{STRUCTURE_1us1| PDB=1us1 | SCENE= }} | | {{STRUCTURE_1us1| PDB=1us1 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1'''
| | ===CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16046623}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16046623 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16046623}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Copper amine oxidase]] | | [[Category: Copper amine oxidase]] |
| [[Category: Vascular adhesion protein-1]] | | [[Category: Vascular adhesion protein-1]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:38 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:26:01 2008'' |