6mzp

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'''Unreleased structure'''
 
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The entry 6mzp is ON HOLD until Paper Publication
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==Zebrafish betaglycan orphan domain structure from orthorhombic crystal form==
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<StructureSection load='6mzp' size='340' side='right'caption='[[6mzp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MZP 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]] 2.1&#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=6mzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzp OCA], [https://pdbe.org/6mzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mzp RCSB], [https://www.ebi.ac.uk/pdbsum/6mzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/E7FDB6_DANRE E7FDB6_DANRE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Betaglycan (BG) and endoglin (ENG), homologous co-receptors of the TGF-beta family, potentiate the signaling activity of TGF-beta2 and inhibin A, and BMP-9 and BMP-10, respectively. BG exists as monomer and forms 1:1 growth factor (GF) complexes, while ENG exists as a dimer and forms 2:1 GF complexes. Herein, the structure of the BG orphan domain (BGO) reveals an insertion that blocks the region that the endoglin orphan domain (ENGO) uses to bind BMP-9, preventing it from binding in the same manner. Using binding studies with domain-deleted forms of TGF-beta and BGO, as well as small-angle X-ray scattering data, BGO is shown to bind its cognate GF in an entirely different manner compared with ENGO. The alternative interfaces likely engender BG and ENG with the ability to selectively bind and target their cognate GFs in a unique temporal-spatial manner, without interfering with one another or other TGF-beta family GFs.
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Authors:
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Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin.,Kim SK, Whitley MJ, Krzysiak TC, Hinck CS, Taylor AB, Zwieb C, Byeon CH, Zhou X, Mendoza V, Lopez-Casillas F, Furey W, Hinck AP Structure. 2019 Jul 16. pii: S0969-2126(19)30231-X. doi:, 10.1016/j.str.2019.06.010. PMID:31327662<ref>PMID:31327662</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6mzp" 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: Danio rerio]]
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[[Category: Large Structures]]
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[[Category: Hinck AP]]
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[[Category: Kim S]]

Current revision

Zebrafish betaglycan orphan domain structure from orthorhombic crystal form

PDB ID 6mzp

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