Related ArticlesHigh-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein.
Biochemistry. 2001 Dec 25;40(51):15520-7
Authors: McNulty JC, Thompson DA, Bolin KA, Wilken J, Barsh GS, Millhauser GL
The agouti-related protein (AGRP) is an endogenous antagonist of the melanocortin receptors MC3R and MC4R found in the hypothalamus and exhibits potent orexigenic (appetite-stimulating) activity. The cysteine-rich C-terminal domain of this protein, corresponding to AGRP(87-132), contains five disulfide bonds and exhibits receptor binding affinity and antagonism equivalent to that of the full-length protein. The three-dimensional structure of this domain has been determined by 1H NMR at 800 MHz. The first 34 residues of AGRP(87-132) are well-ordered and contain a three-stranded antiparallel beta sheet, where the last two strands form a beta hairpin. The relative spatial positioning of the disulfide cross-links demonstrates that the ordered region of AGRP(87-132) adopts the inhibitor cystine knot (ICK) fold previously identified for numerous invertebrate toxins. Interestingly, this may be the first example of a mammalian protein assigned to the ICK superfamily. The hairpin's turn region presents a triplet of residues (Arg-Phe-Phe) known to be essential for melanocortin receptor binding. The structure also suggests that AGRP possesses an additional melanocortin-receptor contact region within a loop formed by the first 16 residues of its C-terminal domain. This specific region shows little sequence homology to the corresponding region of the agouti protein, which is an MC1R antagonist involved in pigmentation. Consideration of these sequence differences, along with recent experiments on mutant and chimeric melanocortin receptors, allows us to postulate that this loop in the first 16 residues of its C-terminal domain confers AGRP's distinct selectivity for MC3R and MC4R.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
Bioorg Chem. 2011 Feb;39(1):59-66
Authors: Borioni A, Bastanzio G, Delfini M, Mustazza C, Sciubba F, Tatti M, Del Giudice MR
The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR. The ligands are...
[NMR paper] Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent p
Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Related Articles Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
Arch Pharm (Weinheim). 2005 Jun;338(5-6):217-28
Authors: Luca S, Heise H, Lange A, Baldus M
Solid-state Nuclear Magnetic Resonance (NMR) provides a general method to study molecular structure and dynamics in a non-crystalline and insoluble environment. We discuss the latest methodological progress to...
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[NMR paper] NMR analysis of in vitro-synthesized proteins without purification: a high-throughput
NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach.
Related Articles NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach.
FEBS Lett. 2002 Jul 31;524(1-3):159-62
Authors: Guignard L, Ozawa K, Pursglove SE, Otting G, Dixon NE
A cell-free protein expression system was established that provides protein samples of adequate concentration and purity for direct NMR analysis. The Escherichia coli peptidyl-prolyl cis-trans isomerase PpiB was expressed in this system...
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[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J Mol Biol. 1997 Oct 3;272(4):573-90
Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...
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[NMR paper] A high-resolution 1H NMR approach for structure determination of membrane peptides an
A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside.
Related Articles A high-resolution 1H NMR approach for structure determination of membrane peptides and proteins in non-deuterated detergent: application to mastoparan X solubilized in n-octylglucoside.
J Biomol NMR. 1995 Jun;5(4):345-52
Authors: Seigneuret M, Lévy D
Application of 1H 2D NMR methods to solubilized membrane proteins and peptides has up to now...
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[NMR paper] High-resolution structure of the phosphorylated form of the histidine-containing phos
High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
J Mol Biol. 1995 Feb 10;246(1):180-93
Authors: van...
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[NMR paper] High-resolution structure of the oligomerization domain of p53 by multidimensional NM
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Related Articles High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a...