1qfv
From Proteopedia
(Difference between revisions)
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1qfv.gif|left|200px]] | ||
| - | + | ==HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS== | |
| - | + | <StructureSection load='1qfv' size='340' side='right'caption='[[1qfv]], [[Resolution|resolution]] 1.36Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1qfv]] 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=1QFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFV FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.36Å</td></tr> | |
| - | + | <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> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfv OCA], [https://pdbe.org/1qfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfv RCSB], [https://www.ebi.ac.uk/pdbsum/1qfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfv ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/HBP2_RHIAP HBP2_RHIAP] | |
| - | + | == 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/qf/1qfv_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1qfv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 1qfv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rhipicephalus appendiculatus]] | [[Category: Rhipicephalus appendiculatus]] | ||
| - | + | [[Category: Adams PL]] | |
| - | [[Category: Adams | + | [[Category: Harlos K]] |
| - | [[Category: Harlos | + | [[Category: Nuttal PA]] |
| - | [[Category: Nuttal | + | [[Category: Paesen GC]] |
| - | [[Category: Paesen | + | [[Category: Stuart DI]] |
| - | [[Category: Stuart | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
HISTAMINE BINDING PROTEIN FROM FEMALE BROWN EAR RHIPICEPHALUS APPENDICULATUS
| |||||||||||
