View source for 2rmg


==Human Urocortin 2==
<StructureSection load='2rmg' size='340' side='right'caption='[[2rmg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rmg]] is a 1 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=2RMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RMG 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=2rmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmg OCA], [https://pdbe.org/2rmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rmg RCSB], [https://www.ebi.ac.uk/pdbsum/2rmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rmg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UCN2_HUMAN UCN2_HUMAN] Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Members of the corticoliberin family include the corticotropin releasing factors (CRFs), sauvagine, the urotensins, and urocortin 1 (Ucn1), which bind to both the CRF receptors CRF-R1 and CRF-R2, and the urocortins 2 (Ucn2) and 3 (Ucn3), which are selective agonists of CRF-R2. Structure activity relationship studies led to several potent and long-acting analogues with selective binding to either one of the receptors. NMR structures of six ligands of this family (the antagonists astressin B and astressin2-B, the agonists stressin1, and the natural ligands human Ucn1, Ucn2, and Ucn3) were determined in DMSO. These six peptides show differences in binding affinities, receptor-selectivity, and NMR structure. Overall, their backbones are alpha-helical, with a small kink or a turn around residues 25-27, resulting in a helix-loop-helix motif. The C-terminal helices are of amphipathic nature, whereas the N-terminal helices vary in their amphipathicity. The C-terminal helices thereby assume a conformation very similar to that of astressin bound to the ECD1 of CRF-R2 recently reported by our group.1 On the basis of an analysis of the observed 3D structures and relative potencies of [Ala]-substituted analogues, it is proposed that both helices could play a crucial role in receptor binding and selectivity. In conclusion, the C-terminal helices may interact along their hydrophobic faces with the ECD1, whereas the entire N-terminal helical surface may be involved in receptor activation. On the basis of the common and divergent features observed in the 3D structures of these ligands, multiple binding models are proposed that may explain their plurality of actions.

Common and divergent structural features of a series of corticotropin releasing factor-related peptides.,Grace CR, Perrin MH, Cantle JP, Vale WW, Rivier JE, Riek R J Am Chem Soc. 2007 Dec 26;129(51):16102-14. Epub 2007 Dec 6. PMID:18052377<ref>PMID:18052377</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rmg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cantle JP]]
[[Category: Grace CRR]]
[[Category: Perrin MH]]
[[Category: Riek R]]
[[Category: Rivier JE]]
[[Category: Vale WW]]