2c10: Difference between revisions

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[[Image:2c10.gif|left|200px]]
[[Image:2c10.gif|left|200px]]


{{Structure
<!--
|PDB= 2c10 |SIZE=350|CAPTION= <scene name='initialview01'>2c10</scene>, resolution 2.50&Aring;
The line below this paragraph, containing "STRUCTURE_2c10", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+D'>AC1</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_2c10| PDB=2c10  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c10 OCA], [http://www.ebi.ac.uk/pdbsum/2c10 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c10 RCSB]</span>
}}


'''THE STRUCTURE OF A TRUNCATED, SOLUBLE VERSION OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE'''
'''THE STRUCTURE OF A TRUNCATED, SOLUBLE VERSION OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE'''
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==Reference==
==Reference==
Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1., Jakobsson E, Nilsson J, Ogg D, Kleywegt GJ, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1550-62. Epub 2005, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16239734 16239734]
Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1., Jakobsson E, Nilsson J, Ogg D, Kleywegt GJ, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1550-62. Epub 2005, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16239734 16239734]
[[Category: Amine oxidase (copper-containing)]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Jakobsson, E.]]
[[Category: Jakobsson, E.]]
[[Category: Kleywegt, G J.]]
[[Category: Kleywegt, G J.]]
[[Category: cell adhesion]]
[[Category: Cell adhesion]]
[[Category: copper]]
[[Category: Copper]]
[[Category: glycoprotein]]
[[Category: Glycoprotein]]
[[Category: metal-binding]]
[[Category: Metal-binding]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: polymorphism]]
[[Category: Polymorphism]]
[[Category: protein-1]]
[[Category: Protein-1]]
[[Category: semicarbazide-sensitive amine oxidase]]
[[Category: Semicarbazide-sensitive amine oxidase]]
[[Category: signal-anchor]]
[[Category: Signal-anchor]]
[[Category: ssao]]
[[Category: Ssao]]
[[Category: tpq]]
[[Category: Tpq]]
[[Category: transmembrane]]
[[Category: Transmembrane]]
[[Category: vap-1]]
[[Category: Vap-1]]
[[Category: vascular adhesion]]
[[Category: Vascular adhesion]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:04:52 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:14:43 2008''

Revision as of 18:04, 3 May 2008

File:2c10.gif

Template:STRUCTURE 2c10

THE STRUCTURE OF A TRUNCATED, SOLUBLE VERSION OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE


Overview

Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs). SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process. The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A. As expected, SSAO is a homodimer with a fold typical of the CuAO family. The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation. The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility. An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane. Carbohydrate moieties are observed at five of six potential N-glycosylation sites. Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity. The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution. Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.

About this Structure

2C10 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1., Jakobsson E, Nilsson J, Ogg D, Kleywegt GJ, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1550-62. Epub 2005, Oct 19. PMID:16239734 Page seeded by OCA on Sat May 3 21:04:52 2008

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