1us1

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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'''
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===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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16046623}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16046623 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16046623}}
==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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:26:01 2008''

Revision as of 23:26, 28 July 2008

Template:STRUCTURE 1us1

CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1

Template:ABSTRACT PUBMED 16046623

About this Structure

1US1 is a Single protein structure of sequence from Homo sapiens. 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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