6jza
From Proteopedia
Structure of Fstl1
Structural highlights
Function[FSTL1_MOUSE] May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity). Publication Abstract from PubMedFstl1 is a TGF-beta superfamily binding protein which involved in many pathological processes. The function of Fstl1 has been widely elucidated, but its structural characterization has not been explored. Here we solved the high-resolution crystal structure of FK domain of murine Fstl1, analyzed its unique characteristics, and investigated its contribution to the function of full-length Fstl1. We found that Fstl1-FK forms a stable dimer in both solution and crystal, which suggest that this protein may function as a dimer during its interaction with TGF-beta, a molecule known to form dimer during activation process. We also found this FK domain is indispensable for the proper function of Fstl1 during the transduction of TGF-beta signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study. Structural and functional study of FK domain of Fstl1.,Li X, Li L, Chang Y, Ning W, Liu X Protein Sci. 2019 Jul 27. doi: 10.1002/pro.3696. PMID:31351024[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Liu, X | Ning, W | Antitumor protein | Development | Dimer | Signaling | Tgf
