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3sek
From Proteopedia
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{{STRUCTURE_3sek| PDB=3sek | SCENE= }} | {{STRUCTURE_3sek| PDB=3sek | SCENE= }} | ||
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===Crystal Structure of the Myostatin:Follistatin-like 3 Complex=== | ===Crystal Structure of the Myostatin:Follistatin-like 3 Complex=== | ||
| + | {{ABSTRACT_PUBMED_022052913}} | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/FSTL3_HUMAN 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== | ||
| + | [[http://www.uniprot.org/uniprot/GDF8_MOUSE GDF8_MOUSE]] Acts specifically as a negative regulator of skeletal muscle growth. [[http://www.uniprot.org/uniprot/FSTL3_HUMAN 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.<ref>PMID:11948405</ref><ref>PMID:15451575</ref><ref>PMID:15574124</ref><ref>PMID:16336961</ref><ref>PMID:17868029</ref><ref>PMID:17878677</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[3sek]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEK OCA]. | [[3sek]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEK OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
Revision as of 07:09, 25 March 2013
Contents |
Crystal Structure of the Myostatin:Follistatin-like 3 Complex
Template:ABSTRACT PUBMED 022052913
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
[GDF8_MOUSE] Acts specifically as a negative regulator of skeletal muscle growth. [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
3sek is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
- ↑ 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
