2mv1
From Proteopedia
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| - | ''' | + | ==Solution NMR structure of Human Relaxin-2== |
| + | <StructureSection load='2mv1' size='340' side='right' caption='[[2mv1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mv1]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MV1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rlx|6rlx]], [[2fhw|2fhw]]</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=2mv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mv1 RCSB], [http://www.ebi.ac.uk/pdbsum/2mv1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/REL2_HUMAN REL2_HUMAN]] Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Relaxin is a member of the relaxin/insulin peptide hormone superfamily and is characterized by a two-chain structure constrained by three disulfide bonds. Relaxin is a pleiotropic hormone and involved in a number of physiological and pathogenic processes, including collagen and cardiovascular regulation and tissue remodelling during pregnancy and cancer. Crystallographic and ultracentrifugation experiments have revealed that the human form of relaxin, H2 relaxin, self-associates into dimers, but the significance of this is poorly understood. Here, we present the NMR structure of a monomeric, amidated form of H2 relaxin and compare its features and behavior in solution to those of native H2 relaxin. The overall structure of H2 relaxin is retained in the monomeric form. H2 relaxin amide is fully active at the relaxin receptor RXFP1 and thus dimerization is not required for biological activity. Analysis of NMR chemical shifts and relaxation parameters identified internal motion in H2 relaxin at the pico-nanosecond and milli-microsecond time scales, which is commonly seen in other relaxin and insulin peptides and might be related to function. | ||
| - | + | Solution Structure, Aggregation Behavior, and Flexibility of Human Relaxin-2.,Haugaard-Kedstrom LM, Hossain MA, Daly NL, Bathgate RA, Rinderknecht E, Wade JD, Craik DJ, Rosengren KJ ACS Chem Biol. 2015 Jan 15. PMID:25547165<ref>PMID:25547165</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: Haugaard-Kedstrom, L | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Haugaard-Kedstrom, L M]] | ||
[[Category: Rosengren, K]] | [[Category: Rosengren, K]] | ||
| + | [[Category: Insulin/relaxin family fold]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Signalling protein]] | ||
Revision as of 15:48, 7 February 2015
Solution NMR structure of Human Relaxin-2
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