This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1us1
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1us1.gif|left|200px]] | + | [[Image:1us1.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1US1 is a [ | + | 1US1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1US1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16046623 16046623] |
[[Category: Amine oxidase (copper-containing)]] | [[Category: Amine oxidase (copper-containing)]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 26: | Line 35: | ||
[[Category: vascular adhesion protein-1]] | [[Category: vascular adhesion protein-1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:56 2008'' |
Revision as of 12:35, 20 March 2008
| |||||||
| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| 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 Thu Mar 20 14:35:56 2008
