2c11

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[[Image:2c11.gif|left|200px]]<br /><applet load="2c11" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c11, resolution 2.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE 2-HYDRAZINOPYRIDINE OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE'''<br />
 
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==Overview==
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==Crystal structure of the 2-hydrazinopyridine of semicarbazide- sensitive amine oxidase==
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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.
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<StructureSection load='2c11' size='340' side='right'caption='[[2c11]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c11_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2C11 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=NDG:'>NDG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=PAQ:'>PAQ</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] Known structural/functional Site: <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C11 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16239734 16239734]
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</div>
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[[Category: Amine oxidase (copper-containing)]]
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<div class="pdbe-citations 2c11" style="background-color:#fffaf0;"></div>
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[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Jakobsson, E.]]
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[[Category: Kleywegt, G.J.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: CU]]
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[[Category: NAG]]
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[[Category: NDG]]
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[[Category: PAQ]]
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[[Category: 2-hydroxypyridine]]
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[[Category: adhesion protein-1]]
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[[Category: cell adhesion]]
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[[Category: copper]]
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[[Category: glycoprotein]]
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[[Category: metal-binding]]
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[[Category: oxidoreductase]]
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[[Category: polymorphism]]
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[[Category: semicarbazide-sensitive amine oxidase]]
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[[Category: signal-anchor]]
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[[Category: ssao]]
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[[Category: tpq]]
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[[Category: transmembrane]]
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[[Category: vap-1]]
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[[Category: vascular]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:30:07 2008''
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==See Also==
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Jakobsson E]]
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[[Category: Kleywegt GJ]]

Current revision

Crystal structure of the 2-hydrazinopyridine of semicarbazide- sensitive amine oxidase

PDB ID 2c11

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