6JZA

Structure of Fstl1

Summary for 6JZA

• Entry DOI: 10.2210/pdb6jza/pdb
• Descriptor: Follistatin-related protein 1 (2 entities in total)
• Functional Keywords: tgf, development, signaling, dimer, antitumor protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 9011.32

Authors

Liu, X.,Ning, W. (deposition date: 2019-04-30, release date: 2019-08-21, Last modification date: 2024-11-13)

Primary citation

Li, X.,Li, L.,Chang, Y.,Ning, W.,Liu, X.
Structural and functional study of FK domain of Fstl1.
Protein Sci., 28:1819-1829, 2019

PubMed Abstract: Fstl1 is a TGF-β 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-β, 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-β signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study.

PubMed: 31351024
DOI: 10.1002/pro.3696

Experimental method

X-RAY DIFFRACTION (2.3 Å)