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5hlz

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Revision as of 10:46, 16 August 2023

Structure of Pro-Activin A Complex at 2.85 A resolution

Structural highlights

5hlz is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.851Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hlz"

Categories: Homo sapiens | Large Structures | Fischer G | Hyvonen M | Wang X

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5HLZ FirstGlance]. <br>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INHBA ([http://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]] 2.851&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hlz OCA], [http://pdbe.org/5hlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hlz RCSB], [http://www.ebi.ac.uk/pdbsum/5hlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hlz 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=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 ==
-[[http://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/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 ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Fischer, G]]
+[[Category: Fischer G]]
-[[Category: Hyvonen, M]]
+[[Category: Hyvonen M]]
-[[Category: Wang, X]]
+[[Category: Wang X]]
-[[Category: Growth factor]]
-[[Category: Precursor]]
-[[Category: Signaling protein]]
-[[Category: Signalling]]

5hlz

From Proteopedia

Revision as of 10:46, 16 August 2023

Structure of Pro-Activin A Complex at 2.85 A resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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