2rmg

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{{STRUCTURE_2rmg| PDB=2rmg | SCENE= }}
{{STRUCTURE_2rmg| PDB=2rmg | SCENE= }}
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'''Human Urocortin 2'''
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===Human Urocortin 2===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_18052377}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 18052377 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18052377}}
==About this Structure==
==About this Structure==
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2RMG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMG OCA].
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2RMG is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMG OCA].
==Reference==
==Reference==
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[[Category: Urocortin]]
[[Category: Urocortin]]
[[Category: Urotensin]]
[[Category: Urotensin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:10:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:26:37 2008''

Revision as of 12:26, 29 July 2008

Image:2rmg.png

Template:STRUCTURE 2rmg

Human Urocortin 2

Template:ABSTRACT PUBMED 18052377

About this Structure

2RMG is a Single protein structure. Full experimental information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 29 15:26:37 2008

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