5E4G
Crystal structure of human growth differentiation factor 11 (GDF-11)
Summary for 5E4G
| Entry DOI | 10.2210/pdb5e4g/pdb |
| Descriptor | Growth/differentiation factor 11, TETRAETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | bone morphogenetic protein 11, bmp-11, gdf 11, hormone, growth factor |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted : O95390 |
| Total number of polymer chains | 1 |
| Total formula weight | 12859.76 |
| Authors | Padyana, A.K.,Vaidialingam, B.,Hayes, D.B.,Gupta, P.,Franti, M.,Farrow, N.A. (deposition date: 2015-10-06, release date: 2016-03-09, Last modification date: 2024-11-06) |
| Primary citation | Padyana, A.K.,Vaidialingam, B.,Hayes, D.B.,Gupta, P.,Franti, M.,Farrow, N.A. Crystal structure of human GDF11. Acta Crystallogr.,Sect.F, 72:160-164, 2016 Cited by PubMed Abstract: Members of the TGF-β family of proteins are believed to play critical roles in cellular signaling processes such as those involved in muscle differentiation. The extent to which individual family members have been characterized and linked to biological function varies greatly. The role of myostatin, also known as growth differentiation factor 8 (GDF8), as an inhibitor of muscle differentiation is well understood through genetic linkages. In contrast, the role of growth differentiation factor 11 (GDF11) is much less well understood. In humans, the mature forms of GDF11 and myostatin are over 94% identical. In order to understand the role that the small differences in sequence may play in the differential signaling of these molecules, the crystal structure of GDF11 was determined to a resolution of 1.50 Å. A comparison of the GDF11 structure with those of other family members reveals that the canonical TGF-β domain fold is conserved. A detailed structural comparison of GDF11 and myostatin shows that several of the differences between these proteins are likely to be localized at interfaces that are critical for the interaction with downstream receptors and inhibitors. PubMed: 26919518DOI: 10.1107/S2053230X16001588 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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