3b4v

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Template:STRUCTURE 3b4v

Contents

X-Ray structure of Activin in complex with FSTL3

Template:ABSTRACT PUBMED 18768470

Disease

[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

[INHBA_HUMAN] Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins. [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]

About this Structure

3b4v is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Stamler R, Keutmann HT, Sidis Y, Kattamuri C, Schneyer A, Thompson TB. The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity. J Biol Chem. 2008 Nov 21;283(47):32831-8. Epub 2008 Sep 2. PMID:18768470 doi:10.1074/jbc.M801266200
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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

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