1us1: Difference between revisions
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==Overview== | ==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 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== | ||
1US1 is a | 1US1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, CU and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1US1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: vascular adhesion protein-1]] | [[Category: vascular adhesion protein-1]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:04:55 2007'' | ||
