6svl

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<StructureSection load='6svl' size='340' side='right'caption='[[6svl]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='6svl' size='340' side='right'caption='[[6svl]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6svl]] is a 18 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SVL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SVL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6svl]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SVL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SVL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYDGF, C19orf10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6svl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6svl OCA], [http://pdbe.org/6svl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6svl RCSB], [http://www.ebi.ac.uk/pdbsum/6svl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6svl ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6svl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6svl OCA], [http://pdbe.org/6svl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6svl RCSB], [http://www.ebi.ac.uk/pdbsum/6svl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6svl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYDGF_HUMAN MYDGF_HUMAN]] Bone marrow-derived monocyte and paracrine-acting protein that promotes cardiac myocyte survival and adaptive angiogenesis for cardiac protection and/or repair after myocardial infarction (MI). Stimulates endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte apoptosis in a PI3K/AKT-dependent signaling pathway (By similarity). Involved in endothelial cell proliferation and angiogenesis (PubMed:25581518).[UniProtKB:Q9CPT4]<ref>PMID:25581518</ref>
[[http://www.uniprot.org/uniprot/MYDGF_HUMAN MYDGF_HUMAN]] Bone marrow-derived monocyte and paracrine-acting protein that promotes cardiac myocyte survival and adaptive angiogenesis for cardiac protection and/or repair after myocardial infarction (MI). Stimulates endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte apoptosis in a PI3K/AKT-dependent signaling pathway (By similarity). Involved in endothelial cell proliferation and angiogenesis (PubMed:25581518).[UniProtKB:Q9CPT4]<ref>PMID:25581518</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Myeloid-derived growth factor (MYDGF) is a paracrine-acting protein that is produced by bone marrow-derived monocytes and macrophages to protect and repair the heart after myocardial infarction (MI). This effect can be used for the development of protein-based therapies for ischemic tissue repair, also beyond the sole application in heart tissue. Here, we report the X-ray structure of MYDGF and identify its functionally relevant receptor binding epitope. MYDGF consists of a 10-stranded beta-sandwich with a folding topology showing no similarities to other cytokines or growth factors. By characterizing the epitope of a neutralizing antibody and utilizing functional assays to study the activity of surface patch-mutations, we were able to localize the receptor interaction interface to a region around two surface tyrosine residues 71 and 73 and an adjacent prominent loop structure of residues 97-101. These findings enable structure-guided protein engineering to develop modified MYDGF variants with potentially improved properties for clinical use.
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Crystal structure and receptor-interacting residues of MYDGF - a protein mediating ischemic tissue repair.,Ebenhoch R, Akhdar A, Reboll MR, Korf-Klingebiel M, Gupta P, Armstrong J, Huang Y, Frego L, Rybina I, Miglietta J, Pekcec A, Wollert KC, Nar H Nat Commun. 2019 Nov 26;10(1):5379. doi: 10.1038/s41467-019-13343-7. PMID:31772377<ref>PMID:31772377</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6svl" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ebenhoch, R]]
[[Category: Ebenhoch, R]]

Revision as of 10:57, 4 December 2019

human Myeloid-derived growth factor (MYDGF) in complex with neutralizing Fab

PDB ID 6svl

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