2wft
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2wft is ON HOLD Authors: Bishop, B., Aricescu, A.R., Harlos, K., O'Callaghan, C.A., Jones, E.Y., Siebold, C. Description: Crystal structure of the ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the human HIP ectodomain== | |
| + | <StructureSection load='2wft' size='340' side='right'caption='[[2wft]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wft]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wfx|2wfx]], [[2wg4|2wg4]], [[2wg3|2wg3]], [[2wfq|2wfq]], [[2wfr|2wfr]]</div></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=2wft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wft OCA], [https://pdbe.org/2wft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wft RCSB], [https://www.ebi.ac.uk/pdbsum/2wft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wft ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/HHIP_HUMAN HHIP_HUMAN]] Modulates hedgehog signaling in several cell types including brain and lung through direct interaction with members of the hedgehog family.<ref>PMID:11472839</ref> <ref>PMID:19561609</ref> | ||
| + | == 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/wf/2wft_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=2wft ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hedgehog (Hh) morphogens have fundamental roles in development, whereas dysregulation of Hh signaling leads to disease. Multiple cell-surface receptors are responsible for transducing and/or regulating Hh signals. Among these, the Hedgehog-interacting protein (Hhip) is a highly conserved, vertebrate-specific inhibitor of Hh signaling. We have solved a series of crystal structures for the human HHIP ectodomain and Desert hedgehog (DHH) in isolation, as well as HHIP in complex with DHH (HHIP-DHH) and Sonic hedgehog (Shh) (HHIP-Shh), with and without Ca2+. The interaction determinants, confirmed by biophysical studies and mutagenesis, reveal previously uncharacterized and distinct functions for the Hh Zn2+ and Ca2+ binding sites--functions that may be common to all vertebrate Hh proteins. Zn2+ makes a key contribution to the Hh-HHIP interface, whereas Ca2+ is likely to prevent electrostatic repulsion between the two proteins, suggesting an important modulatory role. This interplay of several metal binding sites suggests a tuneable mechanism for regulation of Hh signaling. | ||
| - | + | Structural insights into hedgehog ligand sequestration by the human hedgehog-interacting protein HHIP.,Bishop B, Aricescu AR, Harlos K, O'Callaghan CA, Jones EY, Siebold C Nat Struct Mol Biol. 2009 Jul;16(7):698-703. Epub 2009 Jun 28. PMID:19561611<ref>PMID:19561611</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2wft" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Aricescu, A R]] | ||
| + | [[Category: Bishop, B]] | ||
| + | [[Category: Callaghan, C A.O]] | ||
| + | [[Category: Harlos, K]] | ||
| + | [[Category: Jones, E Y]] | ||
| + | [[Category: Siebold, C]] | ||
| + | [[Category: Alternative splicing]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Cytoplasm]] | ||
| + | [[Category: Development]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Egf-like domain]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Hedgehog signalling]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Polymorphism]] | ||
| + | [[Category: Secreted]] | ||
| + | [[Category: Signal transduction]] | ||
| + | [[Category: Signaling protein]] | ||
Current revision
Crystal structure of the human HIP ectodomain
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Categories: Human | Large Structures | Aricescu, A R | Bishop, B | Callaghan, C A.O | Harlos, K | Jones, E Y | Siebold, C | Alternative splicing | Cell membrane | Cytoplasm | Development | Disulfide bond | Egf-like domain | Glycoprotein | Hedgehog signalling | Membrane | Polymorphism | Secreted | Signal transduction | Signaling protein
