1us1
From Proteopedia
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|PDB= 1us1 |SIZE=350|CAPTION= <scene name='initialview01'>1us1</scene>, resolution 2.90Å | |PDB= 1us1 |SIZE=350|CAPTION= <scene name='initialview01'>1us1</scene>, resolution 2.90Å | ||
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1us1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us1 OCA], [http://www.ebi.ac.uk/pdbsum/1us1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1us1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Salminen, T A.]] | [[Category: Salminen, T A.]] | ||
[[Category: Soderholm, A.]] | [[Category: Soderholm, A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NAG]] | ||
[[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:22 2008'' |
Revision as of 21:14, 30 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 00:14:22 2008
