Follistatin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<StructureSection load='3b4v' size='340' side='right' caption='Caption for this structure' scene=''>
+
<StructureSection load='3b4v' size='340' side='right' caption='Human follistatin-like 3 (pink, yellow) complex with activin (grey, green) and sulfate (PDB code [[3b4v]])' scene=''>
== Function ==
== Function ==
Line 5: Line 5:
'''Follistatin''' (Fs1) is a follicle-stimulating hormone inhibiting substance present in ovarian follicular fluid. Fs1 has affinity for [[Activin]] which is neutralized upon binding to Fs1. The interplay between Fs1 and activin represents a regulatory mechanism which affects a variety of cellular processes<ref>PMID:9799587</ref>.<br />
'''Follistatin''' (Fs1) is a follicle-stimulating hormone inhibiting substance present in ovarian follicular fluid. Fs1 has affinity for [[Activin]] which is neutralized upon binding to Fs1. The interplay between Fs1 and activin represents a regulatory mechanism which affects a variety of cellular processes<ref>PMID:9799587</ref>.<br />
-
'''Follistatin-related protein''' (Fst) is highly homologous to Fs1 and binds activin and myostatin but does not contain a heparin-binding motif. Fst contains 2 follistatin domains - containing 10 Cys residues - while Fs1 contains 3 such domains<ref>PMID:11459787</ref>.
+
'''Follistatin-related protein''' (Fstl) is highly homologous to Fs1 and binds activin and myostatin but does not contain a heparin-binding motif. Fst contains 2 follistatin domains - containing 10 Cys residues - while Fs1 contains 3 such domains<ref>PMID:11459787</ref>.
== Relevance ==
== Relevance ==

Revision as of 07:01, 21 May 2020

Human follistatin-like 3 (pink, yellow) complex with activin (grey, green) and sulfate (PDB code 3b4v)

Drag the structure with the mouse to rotate

3D structures of follistatin

Updated on 21-May-2020

References

  1. Phillips DJ, de Kretser DM. Follistatin: a multifunctional regulatory protein. Front Neuroendocrinol. 1998 Oct;19(4):287-322. doi: 10.1006/frne.1998.0169. PMID:9799587 doi:http://dx.doi.org/10.1006/frne.1998.0169
  2. Tortoriello DV, Sidis Y, Holtzman DA, Holmes WE, Schneyer AL. Human follistatin-related protein: a structural homologue of follistatin with nuclear localization. Endocrinology. 2001 Aug;142(8):3426-34. PMID:11459787
  3. Lee SJ, Lee YS, Zimmers TA, Soleimani A, Matzuk MM, Tsuchida K, Cohn RD, Barton ER. Regulation of muscle mass by follistatin and activins. Mol Endocrinol. 2010 Oct;24(10):1998-2008. doi: 10.1210/me.2010-0127. Epub 2010, Sep 1. PMID:20810712 doi:http://dx.doi.org/10.1210/me.2010-0127
  4. Ogura Y, Ouchi N, Ohashi K, Shibata R, Kataoka Y, Kambara T, Kito T, Maruyama S, Yuasa D, Matsuo K, Enomoto T, Uemura Y, Miyabe M, Ishii M, Yamamoto T, Shimizu Y, Walsh K, Murohara T. Therapeutic impact of follistatin-like 1 on myocardial ischemic injury in preclinical models. Circulation. 2012 Oct 2;126(14):1728-38. doi: 10.1161/CIRCULATIONAHA.112.115089. , Epub 2012 Aug 28. PMID:22929303 doi:http://dx.doi.org/10.1161/CIRCULATIONAHA.112.115089

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools