2hlr

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[[Image:2hlr.gif|left|200px]]
 
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==Crystal Structure of the Extracellular Domain of the Type II BMP Receptor==
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The line below this paragraph, containing "STRUCTURE_2hlr", creates the "Structure Box" on the page.
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<StructureSection load='2hlr' size='340' side='right'caption='[[2hlr]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hlr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLR FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.2&#8491;</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=2hlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlr OCA], [https://pdbe.org/2hlr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlr RCSB], [https://www.ebi.ac.uk/pdbsum/2hlr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlr ProSAT]</span></td></tr>
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{{STRUCTURE_2hlr| PDB=2hlr | SCENE= }}
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</table>
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== Function ==
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'''Crystal Structure of the Extracellular Domain of the Type II BMP Receptor'''
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[https://www.uniprot.org/uniprot/Q91WY9_RAT Q91WY9_RAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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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/hl/2hlr_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=2hlr 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 ==
BMPRII is a type II TGF-beta serine threonine kinase receptor which is integral to the bone morphogenetic protein (BMP) signalling pathway. It is known to bind BMP and growth differentiation factor (GDF) ligands, and has overlapping ligand specificity with the activin type II receptor, ActRII. In contrast to activin and TGF-beta type ligands, BMPs bind to type II receptors with lower affinity than type I receptors. Crystals of the BMPRII ectodomain were grown in two different forms, both of which diffracted to high resolution. The tetragonal form exhibited some disorder, whereas the entire polypeptide was seen in the orthorhombic form. The two structures retain the basic three-finger toxin fold of other TGF-beta receptor ectodomains, and share the main hydrophobic patch used by ActRII to bind various ligands. However, they present different conformations of the A-loop at the periphery of the proposed ligand-binding interface, in conjunction with rearrangement of a disulfide bridge within the loop. This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding. Evidence is presented that the two crystal forms represent ligand-bound and free conformations of BMPRII. Comparison with the solved structure of ActRII bound to BMP2 suggests that His87, unique amongst TGF-beta receptors, may play a key role in ligand recognition.
BMPRII is a type II TGF-beta serine threonine kinase receptor which is integral to the bone morphogenetic protein (BMP) signalling pathway. It is known to bind BMP and growth differentiation factor (GDF) ligands, and has overlapping ligand specificity with the activin type II receptor, ActRII. In contrast to activin and TGF-beta type ligands, BMPs bind to type II receptors with lower affinity than type I receptors. Crystals of the BMPRII ectodomain were grown in two different forms, both of which diffracted to high resolution. The tetragonal form exhibited some disorder, whereas the entire polypeptide was seen in the orthorhombic form. The two structures retain the basic three-finger toxin fold of other TGF-beta receptor ectodomains, and share the main hydrophobic patch used by ActRII to bind various ligands. However, they present different conformations of the A-loop at the periphery of the proposed ligand-binding interface, in conjunction with rearrangement of a disulfide bridge within the loop. This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding. Evidence is presented that the two crystal forms represent ligand-bound and free conformations of BMPRII. Comparison with the solved structure of ActRII bound to BMP2 suggests that His87, unique amongst TGF-beta receptors, may play a key role in ligand recognition.
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==About this Structure==
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High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding.,Mace PD, Cutfield JF, Cutfield SM Biochem Biophys Res Commun. 2006 Dec 29;351(4):831-8. Epub 2006 Nov 10. PMID:17094948<ref>PMID:17094948</ref>
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2HLR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLR 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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High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding., Mace PD, Cutfield JF, Cutfield SM, Biochem Biophys Res Commun. 2006 Dec 29;351(4):831-8. Epub 2006 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17094948 17094948]
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</div>
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<div class="pdbe-citations 2hlr" 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: Ovis aries]]
[[Category: Ovis aries]]
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[[Category: Receptor protein serine/threonine kinase]]
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[[Category: Cutfield JF]]
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[[Category: Single protein]]
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[[Category: Cutfield SM]]
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[[Category: Cutfield, J F.]]
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[[Category: Mace PD]]
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[[Category: Cutfield, S M.]]
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[[Category: Mace, P D.]]
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[[Category: Bmp receptor]]
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[[Category: Tgf-beta]]
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[[Category: Three-finger toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:26:20 2008''
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Current revision

Crystal Structure of the Extracellular Domain of the Type II BMP Receptor

PDB ID 2hlr

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