Crystal structure of human GDF11
| Autor: | Bhamini Vaidialingam, Michael Franti, Priyanka Gupta, Neil A. Farrow, Anil Kumar Padyana, David B. Hayes |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical 0301 basic medicine Cell signaling TGF alpha Biophysics Myostatin Biology Crystallography X-Ray Biochemistry Research Communications 03 medical and health sciences Structural Biology Genetics Humans Protein Structure Quaternary Receptor 030102 biochemistry & molecular biology Growth differentiation factor TGF beta receptor 2 Condensed Matter Physics Protein Structure Tertiary Cell biology Growth Differentiation Factors 030104 developmental biology Structural Homology Protein Transforming growth factor beta 3 Bone Morphogenetic Proteins GDF11 biology.protein |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 72:160-164 |
| ISSN: | 2053-230X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|