2fhw

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(New page: 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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[[Image:2fhw.gif|left|200px]]<br />
 
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<applet load="2fhw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fhw" />
 
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'''Solution structure of human relaxin-3'''<br />
 
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==Overview==
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==Solution structure of human relaxin-3==
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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.
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<StructureSection load='2fhw' size='340' side='right'caption='[[2fhw]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2FHW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FHW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16365033 16365033]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2fhw" style="background-color:#fffaf0;"></div>
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[[Category: Craik, D.J.]]
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== References ==
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[[Category: Rosengren, K.J.]]
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<references/>
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[[Category: insulin/relaxin super-family fold]]
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__TOC__
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</StructureSection>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:05:33 2007''
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Craik DJ]]
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[[Category: Rosengren KJ]]

Current revision

Solution structure of human relaxin-3

PDB ID 2fhw

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