Structural highlights
FunctionGDF11_HUMAN Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. Play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern. Publication Abstract from PubMedMembers of the TGF-beta 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 A. A comparison of the GDF11 structure with those of other family members reveals that the canonical TGF-beta 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. Crystal structure of human GDF11.,Padyana AK, Vaidialingam B, Hayes DB, Gupta P, Franti M, Farrow NA Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):160-4. doi:, 10.1107/S2053230X16001588. Epub 2016 Feb 16. PMID:26919518[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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