Related ArticlesNMR structure of the first extracellular domain of corticotropin releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist.
J Biol Chem. 2010 Sep 15;
Authors: Grace CR, Perrin MH, Gulyas J, Rivier JE, Vale WW, Riek R
The corticotropin releasing factor (CRF) peptide hormone family members coordinate endocrine, behavioral, autonomic and metabolic responses to stress and play important roles within the cardiovascular, gastrointestinal and central nervous systems, among others. The actions of the peptides are mediated by activation of two G-protein coupled receptors (GPCRs) of the B1 family, CRF receptors 1 and 2 (CRF-R1 and CRF-R2α,β). The recently reported 3D structures of the first extracellular domain (ECD1) of both CRF-R1 and CRF-R2β (1,2) complexed with peptide antagonists provided a starting point in understanding the binding between CRF ligands and receptors at a molecular level. We now report the 3D NMR structure of the ECD1 of human CRF-R1 complexed with a high affinity agonist, αhcCRF. In the structure of the complex, the C-terminal residues (23-41) of αhcCRF bind to the ECD1 of CRF-R1 in a helical conformation mainly along the peptide's hydrophobic face in a manner similar to that of the antagonists in their corresponding ECD1-complex structures. Unique to this study is the observation that complex formation between an agonist and the ECD1-CRF-R1 promotes the helical conformation of the N-terminus of the former, important for receptor activation (3,4).
PMID: 20843795 [PubMed - as supplied by publisher]
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/rGTPGWIkyp0
More...
nmrlearner
Journal club
0
10-21-2011 09:52 AM
[NMR paper] Solution NMR structure investigation for releasing mechanism of neocarzinostatin chro
Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein.
Related Articles Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from the holoprotein.
J Biol Chem. 2005 Mar 25;280(12):11340-6
Authors: Takashima H, Yoshida T, Ishino T, Hasuda K, Ohkubo T, Kobayashi Y
Holo-neocarzinostatin (holo-NCS) is a complex protein carrying the anti-tumor active enediyne ring chromophore by a scaffold consisting of an immunoglobulin-like seven-stranded...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] NMR structure and peptide hormone binding site of the first extracellular domain of a
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Related Articles NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41
Authors: Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands'...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] Structural characterization by NMR of the natively unfolded extracellular domain of b
Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan.
Related Articles Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan.
Biochemistry. 2003 Nov 25;42(46):13717-24
Authors: Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO
Dystroglycan (DG) is an adhesion molecule playing a...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
Related Articles Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic ace
Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit.
Related Articles Yeast expression and NMR analysis of the extracellular domain of muscle nicotinic acetylcholine receptor alpha subunit.
J Biol Chem. 2002 Apr 12;277(15):12613-21
Authors: Yao Y, Wang J, Viroonchatapan N, Samson A, Chill J, Rothe E, Anglister J, Wang ZZ
The alpha subunit of the nicotinic acetylcholine receptor (AChR) from Torpedo electric organ and mammalian muscle contains high affinity binding sites for...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Conformational differences of ovine and human corticotropin releasing hormone. A CD,
Conformational differences of ovine and human corticotropin releasing hormone. A CD, IR, NMR and dynamic light scattering study.
Related Articles Conformational differences of ovine and human corticotropin releasing hormone. A CD, IR, NMR and dynamic light scattering study.
Int J Pept Protein Res. 1996 May;47(5):383-93
Authors: Dathe M, Fabian H, Gast K, Zirwer D, Winter R, Beyermann M, Schümann M, Bienert M
The differences in the conformational properties of ovine (o) and human (h) CRH in aqueous solution, structure-inducing TFE and in the...