2fhw: Difference between revisions
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New page: left|200px<br /> <applet load="2fhw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fhw" /> '''Solution structure of human relaxin-3'''<br... |
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== | ==Solution structure of human relaxin-3== | ||
Relaxin-3 is the most recently discovered member of the relaxin family of | <StructureSection load='2fhw' size='340' side='right'caption='[[2fhw]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2fhw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FHW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhw OCA], [https://pdbe.org/2fhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fhw RCSB], [https://www.ebi.ac.uk/pdbsum/2fhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fhw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/REL3_HUMAN REL3_HUMAN] May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 (GPCR135) and relaxin-3 receptor-2 (GPCR142). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Relaxin-3 is the most recently discovered member of the relaxin family of peptide hormones. In contrast to relaxin-1 and -2, whose main functions are associated with pregnancy, relaxin-3 is involved in neuropeptide signaling in the brain. Here, we report the solution structure of human relaxin-3, the first structure of a relaxin family member to be solved by NMR methods. Overall, relaxin-3 adopts an insulin-like fold, but the structure differs crucially from the crystal structure of human relaxin-2 near the B-chain terminus. In particular, the B-chain C terminus folds back, allowing Trp(B27) to interact with the hydrophobic core. This interaction partly blocks the conserved RXXXRXXI motif identified as a determinant for the interaction with the relaxin receptor LGR7 and may account for the lower affinity of relaxin-3 relative to relaxin for this receptor. This structural feature is likely important for the activation of its endogenous receptor, GPCR135. | |||
Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3.,Rosengren KJ, Lin F, Bathgate RA, Tregear GW, Daly NL, Wade JD, Craik DJ J Biol Chem. 2006 Mar 3;281(9):5845-51. Epub 2005 Dec 19. PMID:16365033<ref>PMID:16365033</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2fhw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Craik DJ]] | |||
[[Category: Rosengren KJ]] | |||
Latest revision as of 16:36, 13 December 2023
Solution structure of human relaxin-3
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