1qft

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(New page: 200px<br /><applet load="1qft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qft, resolution 1.25&Aring;" /> '''HISTAMINE BINDING PR...)
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[[Image:1qft.gif|left|200px]]<br /><applet load="1qft" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qft, resolution 1.25&Aring;" />
 
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'''HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS'''<br />
 
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==Overview==
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==HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS==
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High-affinity histamine-binding proteins (HBPs) were discovered in the, saliva of Rhipicephalus appendiculatus ticks. Their ability to outcompete, histamine receptors indicates that they suppress inflammation during blood, feeding. The crystal structure of a histamine-bound HBP, determined at, 1.25 A resolution, reveals a lipocalin fold novel in containing two, binding sites for the same ligand. The sites are orthogonally arranged and, highly rigid and form an internal surface of unusual polar character that, complements the physicochemical properties of histamine. As soluble, receptors of histamine, HBPs offer a new strategy for controlling, histamine-based diseases.
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<StructureSection load='1qft' size='340' side='right'caption='[[1qft]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qft]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFT 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]] 1.25&#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=HSM:HISTAMINE'>HSM</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=1qft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qft OCA], [https://pdbe.org/1qft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qft RCSB], [https://www.ebi.ac.uk/pdbsum/1qft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qft ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HBP2_RHIAP HBP2_RHIAP]
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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/qf/1qft_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=1qft 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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High-affinity histamine-binding proteins (HBPs) were discovered in the saliva of Rhipicephalus appendiculatus ticks. Their ability to outcompete histamine receptors indicates that they suppress inflammation during blood feeding. The crystal structure of a histamine-bound HBP, determined at 1.25 A resolution, reveals a lipocalin fold novel in containing two binding sites for the same ligand. The sites are orthogonally arranged and highly rigid and form an internal surface of unusual polar character that complements the physicochemical properties of histamine. As soluble receptors of histamine, HBPs offer a new strategy for controlling histamine-based diseases.
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==About this Structure==
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Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure.,Paesen GC, Adams PL, Harlos K, Nuttall PA, Stuart DI Mol Cell. 1999 May;3(5):661-71. PMID:10360182<ref>PMID:10360182</ref>
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1QFT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhipicephalus_appendiculatus Rhipicephalus appendiculatus] with HSM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFT 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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Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure., Paesen GC, Adams PL, Harlos K, Nuttall PA, Stuart DI, Mol Cell. 1999 May;3(5):661-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10360182 10360182]
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</div>
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<div class="pdbe-citations 1qft" style="background-color:#fffaf0;"></div>
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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: Large Structures]]
[[Category: Rhipicephalus appendiculatus]]
[[Category: Rhipicephalus appendiculatus]]
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[[Category: Single protein]]
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[[Category: Adams PL]]
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[[Category: Adams, P.L.]]
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[[Category: Harlos K]]
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[[Category: Harlos, K.]]
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[[Category: Nuttal PA]]
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[[Category: Nuttal, P.A.]]
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[[Category: Paesen GC]]
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[[Category: Paesen, G.C.]]
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[[Category: Stuart DI]]
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[[Category: Stuart, D.I.]]
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[[Category: HSM]]
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[[Category: lipocalin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:39:04 2007''
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Current revision

HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS

PDB ID 1qft

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