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| | <StructureSection load='2p6a' size='340' side='right'caption='[[2p6a]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='2p6a' size='340' side='right'caption='[[2p6a]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2p6a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P6A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2p6a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P6A FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INHBA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FST ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6a OCA], [https://pdbe.org/2p6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p6a RCSB], [https://www.ebi.ac.uk/pdbsum/2p6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p6a ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6a OCA], [https://pdbe.org/2p6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p6a RCSB], [https://www.ebi.ac.uk/pdbsum/2p6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p6a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/INHBA_HUMAN 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. [[https://www.uniprot.org/uniprot/FST_HUMAN FST_HUMAN]] Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
| + | [https://www.uniprot.org/uniprot/INHBA_HUMAN 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jardetzky, T S]] | + | [[Category: Jardetzky TS]] |
| - | [[Category: Lerch, T F]] | + | [[Category: Lerch TF]] |
| - | [[Category: Shimasaki, S]] | + | [[Category: Shimasaki S]] |
| - | [[Category: Woodruff, T K]] | + | [[Category: Woodruff TK]] |
| - | [[Category: Activin]]
| + | |
| - | [[Category: Follistatin]]
| + | |
| - | [[Category: Inhibin]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Tgf-beta]]
| + | |
| Structural highlights
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Follistatin (FS) regulates transforming growth factor-beta superfamily ligands and is necessary for normal embryonic and ovarian follicle development. Follistatin is expressed as two splice variants (FS288 and FS315). Previous studies indicated differences in heparin binding between FS288 and FS315, potentially influencing the physiological functions and locations of these isoforms. We have determined the structure of the FS315-activin A complex and quantitatively compared heparin binding by the two isoforms. The FS315 complex structure shows that both isoforms inhibit activin similarly, but FS315 exhibits movements within follistatin domain 3 (FSD3) apparently linked to binding of the C-terminal extension. Surprisingly, the binding affinities of FS288 and FS315 for heparin are similar at lower ionic strengths with FS315 binding decreasing more sharply as a function of salt concentration. When bound to activin, FS315 binds heparin similarly to the FS288 isoform, consistent with the structure of the complex, in which the acidic residues of the C-terminal extension cannot interact with the heparin-binding site. Activin-induced binding of heparin is unique to the FS315 isoform and may stimulate clearance of FS315 complexes.
Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions.,Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. PMID:17409095[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS. Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions. J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. PMID:17409095 doi:10.1074/jbc.M700737200
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