2o8z

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[[Image:2o8z.gif|left|200px]]
[[Image:2o8z.gif|left|200px]]
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{{Structure
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|PDB= 2o8z |SIZE=350|CAPTION= <scene name='initialview01'>2o8z</scene>
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The line below this paragraph, containing "STRUCTURE_2o8z", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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{{STRUCTURE_2o8z| PDB=2o8z | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8z OCA], [http://www.ebi.ac.uk/pdbsum/2o8z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o8z RCSB]</span>
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'''Bound Structure of CRF1 Extracellular Domain Antagonist'''
'''Bound Structure of CRF1 Extracellular Domain Antagonist'''
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==About this Structure==
==About this Structure==
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2O8Z is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8Z OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8Z OCA].
==Reference==
==Reference==
NMR structural characterization of a minimal peptide antagonist bound to the extracellular domain of the corticotropin-releasing factor1 receptor., Mesleh MF, Shirley WA, Heise CE, Ling N, Maki RA, Laura RP, J Biol Chem. 2007 Mar 2;282(9):6338-46. Epub 2006 Dec 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17192263 17192263]
NMR structural characterization of a minimal peptide antagonist bound to the extracellular domain of the corticotropin-releasing factor1 receptor., Mesleh MF, Shirley WA, Heise CE, Ling N, Maki RA, Laura RP, J Biol Chem. 2007 Mar 2;282(9):6338-46. Epub 2006 Dec 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17192263 17192263]
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[[Category: Protein complex]]
 
[[Category: Heise, C E.]]
[[Category: Heise, C E.]]
[[Category: Laura, R P.]]
[[Category: Laura, R P.]]
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[[Category: Mesleh, M F.]]
[[Category: Mesleh, M F.]]
[[Category: Shirley, W A.]]
[[Category: Shirley, W A.]]
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[[Category: crf]]
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[[Category: Crf]]
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[[Category: ecd]]
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[[Category: Ecd]]
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[[Category: extracellular domain]]
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[[Category: Extracellular domain]]
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[[Category: gpcr]]
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[[Category: Gpcr]]
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[[Category: helical]]
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[[Category: Helical]]
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[[Category: peptide ligand]]
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[[Category: Peptide ligand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:28:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:14:27 2008''
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Revision as of 07:28, 4 May 2008

Image:2o8z.gif

Template:STRUCTURE 2o8z

Bound Structure of CRF1 Extracellular Domain Antagonist


Overview

Natural peptide agonists of corticotrophin-releasing factor (CRF) receptors bind to the receptor by a two-site mechanism as follows: the carboxyl end of the ligand binds the N-terminal extracellular domain (ECD) of the receptor and the amino portion of the ligand binds the extracellular face of the seven transmembrane region. Recently, peptide antagonists homologous to the 12 C-terminal residues of CRF have been derived, which bind the CRF(1) receptor through an interaction with the ECD. Here we characterized the binding of a minimal 12-residue peptide antagonist while bound to the isolated ECD of the CRF(1) receptor. We have expressed and purified soluble and properly folded ECD independent from the seven-transmembrane region as a thioredoxin fusion protein in Escherichia coli. A model of the peptide antagonist, cyclic corticotrophin-releasing factor residues 30-41 (cCRF(30-41)), was calculated while bound to the recombinant ECD using transferred nuclear Overhauser effect spectroscopy. Although the peptide is unstructured in solution, it adopts an alpha-helical conformation when bound to the ECD. Residues of cCRF(30-41) comprising the binding interface with the ECD were mapped using saturation transfer difference NMR. Two hydrophobic residues (Met(38) and Ile(41)) as well as two amide groups (Asn(34) and the C-terminal amide) on one face of the helix defined the binding epitope of the antagonist. This epitope may be used as a starting point for development of non-peptide antagonists targeting the ECD of this receptor.

About this Structure

Full crystallographic information is available from OCA.

Reference

NMR structural characterization of a minimal peptide antagonist bound to the extracellular domain of the corticotropin-releasing factor1 receptor., Mesleh MF, Shirley WA, Heise CE, Ling N, Maki RA, Laura RP, J Biol Chem. 2007 Mar 2;282(9):6338-46. Epub 2006 Dec 27. PMID:17192263 Page seeded by OCA on Sun May 4 10:28:29 2008

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