2c10: Difference between revisions

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


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==The structure of a truncated, soluble version of semicarbazide- sensitive amine oxidase==
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<StructureSection load='2c10' size='340' side='right'caption='[[2c10]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c10]] 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=2C10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C10 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]] 2.5&#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=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr>
{{STRUCTURE_2c10|  PDB=2c10  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c10 OCA], [https://pdbe.org/2c10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c10 RCSB], [https://www.ebi.ac.uk/pdbsum/2c10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c10 ProSAT]</span></td></tr>
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== 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]]
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    <text>to colour the structure by Evolutionary Conservation</text>
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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=2c10 ConSurf].
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== 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.


===THE STRUCTURE OF A TRUNCATED, SOLUBLE VERSION 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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16239734 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16239734}}
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</StructureSection>
==About this Structure==
2C10 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=2C10 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:[http://www.ncbi.nlm.nih.gov/pubmed/16239734 16239734]
[[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: Cell adhesion]]
[[Category: Copper]]
[[Category: Glycoprotein]]
[[Category: Metal-binding]]
[[Category: Oxidoreductase]]
[[Category: Polymorphism]]
[[Category: Protein-1]]
[[Category: Semicarbazide-sensitive amine oxidase]]
[[Category: Signal-anchor]]
[[Category: Ssao]]
[[Category: Tpq]]
[[Category: Transmembrane]]
[[Category: Vap-1]]
[[Category: Vascular adhesion]]
 
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