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- | [[Image:2c11.gif|left|200px]] | |
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- | <!-- | + | ==Crystal structure of the 2-hydrazinopyridine of semicarbazide- sensitive amine oxidase== |
- | The line below this paragraph, containing "STRUCTURE_2c11", creates the "Structure Box" on the page.
| + | <StructureSection load='2c11' size='340' side='right'caption='[[2c11]], [[Resolution|resolution]] 2.90Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2c11]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C11 FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PAQ:2-OXY-4-HYDROXY-5-(2-HYDRAZINOPYRIDINE)PHENYLALANINE'>PAQ</scene></td></tr> |
- | {{STRUCTURE_2c11| PDB=2c11 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c11 OCA], [https://pdbe.org/2c11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c11 RCSB], [https://www.ebi.ac.uk/pdbsum/2c11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c11 ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/AOC3_HUMAN AOC3_HUMAN] Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis.<ref>PMID:9653080</ref> <ref>PMID:17400359</ref> <ref>PMID:19588076</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c11_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c11 ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | 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. |
| | | |
- | '''CRYSTAL STRUCTURE OF THE 2-HYDRAZINOPYRIDINE OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE'''
| + | 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<ref>PMID:16239734</ref> |
- | | + | |
- | | + | |
- | ==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==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | 2C11 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=2C11 OCA].
| + | </div> |
| + | <div class="pdbe-citations 2c11" style="background-color:#fffaf0;"></div> |
| | | |
- | ==Reference== | + | ==See Also== |
- | 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]
| + | *[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]] |
| + | == References == |
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Jakobsson, E.]] | + | [[Category: Jakobsson E]] |
- | [[Category: Kleywegt, G J.]] | + | [[Category: Kleywegt GJ]] |
- | [[Category: 2-hydroxypyridine]]
| + | |
- | [[Category: Adhesion protein-1]]
| + | |
- | [[Category: Cell adhesion]]
| + | |
- | [[Category: Copper]]
| + | |
- | [[Category: Glycoprotein]]
| + | |
- | [[Category: Metal-binding]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Polymorphism]]
| + | |
- | [[Category: Semicarbazide-sensitive amine oxidase]]
| + | |
- | [[Category: Signal-anchor]]
| + | |
- | [[Category: Ssao]]
| + | |
- | [[Category: Tpq]]
| + | |
- | [[Category: Transmembrane]]
| + | |
- | [[Category: Vap-1]]
| + | |
- | [[Category: Vascular]]
| + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:04:55 2008''
| + | |
| Structural highlights
2c11 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 2.9Å |
Ligands: | , , , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AOC3_HUMAN Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S. Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. PMID:9653080
- ↑ Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C. Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. PMID:17400359 doi:http://dx.doi.org/10.1016/j.biochi.2007.02.013
- ↑ Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K. The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. doi: 10.1007/s00018-009-0076-5. Epub , 2009 Jul 9. PMID:19588076 doi:http://dx.doi.org/10.1007/s00018-009-0076-5
- ↑ Jakobsson E, Nilsson J, Ogg D, Kleywegt GJ. Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1550-62. Epub 2005, Oct 19. PMID:16239734 doi:http://dx.doi.org/10.1107/S0907444905028805
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