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1us1
From Proteopedia
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| - | [[Image:1us1.gif|left|200px]]<br /> | + | [[Image:1us1.gif|left|200px]]<br /><applet load="1us1" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1us1" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1us1, resolution 2.90Å" /> | caption="1us1, resolution 2.90Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] | + | 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] Known structural/functional Site: <scene name='pdbsite=AC1:Nag Binding Site For Chain B'>AC1</scene>. 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 Tue Dec 18 18:08:42 2007'' |
Revision as of 15:58, 18 December 2007
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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 NAG, CU and CA 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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