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1us1

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[[Image:1us1.gif|left|200px]]<br />
 
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<applet load="1us1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1us1, resolution 2.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN VASCULAR ADHESION PROTEIN-1'''<br />
 
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==Overview==
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==Crystal structure of human vascular adhesion protein-1==
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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.
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<StructureSection load='1us1' size='340' side='right'caption='[[1us1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1us1]] is a 2 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=1US1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1US1 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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>
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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=1us1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1us1 OCA], [https://pdbe.org/1us1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1us1 RCSB], [https://www.ebi.ac.uk/pdbsum/1us1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1us1 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/us/1us1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1us1 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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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.
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==About this Structure==
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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<ref>PMID:16046623</ref>
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1US1 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1US1 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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16046623 16046623]
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</div>
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[[Category: Amine oxidase (copper-containing)]]
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<div class="pdbe-citations 1us1" style="background-color:#fffaf0;"></div>
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[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Airenne, T.T.]]
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[[Category: Johnson, M.S.]]
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[[Category: Kidron, H.]]
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[[Category: Nymalm, Y.]]
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[[Category: Salminen, T.A.]]
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[[Category: Soderholm, A.]]
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[[Category: CA]]
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[[Category: CU]]
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[[Category: NAG]]
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[[Category: copper amine oxidase]]
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[[Category: vascular adhesion protein-1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:10:06 2007''
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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: Airenne TT]]
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[[Category: Johnson MS]]
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[[Category: Kidron H]]
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[[Category: Nymalm Y]]
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[[Category: Salminen TA]]
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[[Category: Soderholm A]]

Current revision

Crystal structure of human vascular adhesion protein-1

PDB ID 1us1

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