2fhw: Difference between revisions
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[[ | ==Solution structure of human relaxin-3== | ||
<StructureSection load='2fhw' size='340' side='right' caption='[[2fhw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2fhw]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FHW FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fhw RCSB], [http://www.ebi.ac.uk/pdbsum/2fhw PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
[[Category: Rosengren, K J.]] | [[Category: Rosengren, K J.]] | ||
[[Category: Insulin/relaxin super-family fold]] | [[Category: Insulin/relaxin super-family fold]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 15:26, 12 October 2014
Solution structure of human relaxin-3
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