Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Structural highlights
2kcx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
FSTL3_HUMAN Note=A chromosomal aberration involving FSTL3 is found in a case of B-cell chronic lymphocytic leukemia. Translocation t(11;19)(q13;p13) with CCDN1.
Function
FSTL3_HUMAN Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiationc. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10.[1][2][3][4][5][6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Bartholin L, Maguer-Satta V, Hayette S, Martel S, Gadoux M, Corbo L, Magaud JP, Rimokh R. Transcription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A function. Oncogene. 2002 Mar 28;21(14):2227-35. PMID:11948405 doi:10.1038/sj.onc.1205294
↑Maguer-Satta V, Rimokh R. FLRG, member of the follistatin family, a new player in hematopoiesis. Mol Cell Endocrinol. 2004 Oct 15;225(1-2):109-18. PMID:15451575 doi:10.1016/j.mce.2004.07.009
↑Bartholin L, Destaing O, Forissier S, Martel S, Maguer-Satta V, Jurdic P, Rimokh R. FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation. Biol Cell. 2005 Jul;97(7):577-88. PMID:15574124 doi:10.1042/BC20040506
↑Maguer-Satta V, Forissier S, Bartholin L, Martel S, Jeanpierre S, Bachelard E, Rimokh R. A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG and follistatin. Exp Cell Res. 2006 Feb 15;312(4):434-42. Epub 2005 Dec 5. PMID:16336961 doi:10.1016/j.yexcr.2005.11.006
↑Forissier S, Razanajaona D, Ay AS, Martel S, Bartholin L, Rimokh R. AF10-dependent transcription is enhanced by its interaction with FLRG. Biol Cell. 2007 Oct;99(10):563-71. PMID:17868029
↑Takehara-Kasamatsu Y, Tsuchida K, Nakatani M, Murakami T, Kurisaki A, Hashimoto O, Ohuchi H, Kurose H, Mori K, Kagami S, Noji S, Sugino H. Characterization of follistatin-related gene as a negative regulatory factor for activin family members during mouse heart development. J Med Invest. 2007 Aug;54(3-4):276-88. PMID:17878677
