6SVK
human Myeloid-derived growth factor (MYDGF)
Summary for 6SVK
| Entry DOI | 10.2210/pdb6svk/pdb |
| Descriptor | Myeloid-derived growth factor, MALONATE ION (3 entities in total) |
| Functional Keywords | mydgf, growth factor, orphan ligand, ischemic tissue repair, unique cytokine fold, reduces scar size after myocardial infarction, cytokine |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 31811.53 |
| Authors | Ebenhoch, R.,Nar, H. (deposition date: 2019-09-18, release date: 2019-11-27, Last modification date: 2024-11-13) |
| Primary citation | Ebenhoch, R.,Akhdar, A.,Reboll, M.R.,Korf-Klingebiel, M.,Gupta, P.,Armstrong, J.,Huang, Y.,Frego, L.,Rybina, I.,Miglietta, J.,Pekcec, A.,Wollert, K.C.,Nar, H. Crystal structure and receptor-interacting residues of MYDGF - a protein mediating ischemic tissue repair. Nat Commun, 10:5379-5379, 2019 Cited by PubMed Abstract: 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 β-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. PubMed: 31772377DOI: 10.1038/s41467-019-13343-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.604 Å) |
Structure validation
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