View source for 5hlz


==Structure of Pro-Activin A Complex at 2.85 A resolution==
<StructureSection load='5hlz' size='340' side='right'caption='[[5hlz]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hlz]] is a 8 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=5HLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HLZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.851&#8491;</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=5hlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hlz OCA], [https://pdbe.org/5hlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hlz RCSB], [https://www.ebi.ac.uk/pdbsum/5hlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hlz ProSAT]</span></td></tr>
</table>
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Activins are growth factors with multiple roles in the development and homeostasis. Like all TGF-beta family of growth factors, activins are synthesized as large precursors from which mature dimeric growth factors are released proteolytically. Here we have studied the activation of activin A and determined crystal structures of the unprocessed precursor and of the cleaved pro-mature complex. Replacing the natural furin cleavage site with a HRV 3C protease site, we show how the protein gains its bioactivity after proteolysis and is as active as the isolated mature domain. The complex remains associated in conditions used for biochemical analysis with a dissociation constant of 5 nM, but the pro-domain can be actively displaced from the complex by follistatin. Our high-resolution structures of pro-activin A share features seen in the pro-TGF-beta1 and pro-BMP-9 structures, but reveal a new oligomeric arrangement, with a domain-swapped, cross-armed conformation for the protomers in the dimeric protein.

Structure and activation of pro-activin A.,Wang X, Fischer G, Hyvonen M Nat Commun. 2016 Jul 4;7:12052. doi: 10.1038/ncomms12052. PMID:27373274<ref>PMID:27373274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hlz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Activin|Activin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Fischer G]]
[[Category: Hyvonen M]]
[[Category: Wang X]]