1pu4: Difference between revisions
New page: left|200px<br /> <applet load="1pu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pu4, resolution 3.20Å" /> '''Crystal structure o... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1pu4.gif|left|200px]]<br /> | [[Image:1pu4.gif|left|200px]]<br /><applet load="1pu4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1pu4" size=" | |||
caption="1pu4, resolution 3.20Å" /> | caption="1pu4, resolution 3.20Å" /> | ||
'''Crystal structure of human vascular adhesion protein-1'''<br /> | '''Crystal structure of human vascular adhesion protein-1'''<br /> | ||
==Overview== | ==Overview== | ||
The expression of human vascular adhesion protein-1 (hVAP-1) is induced at | 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== | ||
1PU4 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] Full crystallographic information is available from [http:// | 1PU4 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 <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CA:'>CA</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PU4 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Airenne, T | [[Category: Airenne, T T.]] | ||
[[Category: Salminen, T | [[Category: Salminen, T A.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CU]] | [[Category: CU]] | ||
| Line 22: | Line 21: | ||
[[Category: amine oxidase]] | [[Category: amine oxidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:33 2008'' | ||
Revision as of 15:32, 21 February 2008
|
Crystal structure of human vascular adhesion protein-1
OverviewOverview
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 StructureAbout this Structure
1PU4 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.
ReferenceReference
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 Feb 21 14:32:33 2008