Related ArticlesConformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution.
Chembiochem. 2015 Jan 19;16(2):214-8
Authors: Roche J, Louis JM, Bax A
Abstract
Flexibility of the glycine-rich flaps is known to be essential for catalytic activity of the HIV-1 protease, but their exact conformations at the different stages of the enzymatic pathway remain subject to much debate. Although hundreds of crystal structures of protease-inhibitor complexes have been solved, only about a dozen inhibitor-free protease structures have been reported. These latter structures reveal a large diversity of flap conformations, ranging from closed to semi-open to wide open. To evaluate the average structure in solution, we measured residual dipolar couplings (RDCs) and compared these to values calculated for crystal structures representative of the closed, semi-open, and wide-open states. The RDC data clearly indicate that the inhibitor-free protease, on average, adopts a closed conformation in solution that is very similar to the inhibitor-bound state. By contrast, a highly drug-resistant protease mutant, PR20, adopts the wide-open flap conformation.
[NMR paper] Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
J Pharm Biomed Anal. 2012 Nov;70:609-13
Authors: Busacca CA, Jones PJ, Campbell SJ, Saha AK, Gonnella NC, Senanayake CH
Abstract
The ability of the macrocyclic HCV protease inhibitor BILN 2061 to bind different...
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Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
Combined X-ray, NMR and kinetic analyses reveal uncommon binding characteristics of the HCV NS3-NS4A protease inhibitor BI 201335.
J Biol Chem. 2011 Jan 26;
Authors: Lemke CT, Goudreau N, Zhao S, Hucke O, Thibeault D, Llinás-Brunet M, White PW
Hepatitis C virus (HCV) infection, a major cause of liver disease world-wide, is curable but currently approved therapies have suboptimal efficacy. Supplementing these therapies...
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01-29-2011 12:35 PM
[NMR paper] The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--fr
The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--from the NMR tube to the clinic.
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Biopolymers. 2004;76(4):309-23
Authors: Tsantrizos YS
The virally encoded serine protease NS3/NS4A is essential to the life cycle of the hepatitis C virus (HCV), an important human pathogen causing chronic hepatitis, cirrhosis of the liver, and hepatocellular carcinoma. Until very recently, the...
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[NMR paper] The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor
The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
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Biopolymers. 2003 Jun;69(2):201-15
Authors: Miskolzie M, Kotovych G
The tertiary structure of the pain modulating and anti-opiate neuropeptide, human neuropeptide AF (NPAF) (the sequence is AGEGLNSQFWSLAAPQRF-NH(2)), was determined by (1)H-NMR. The structure of NPAF was determined in two solvent systems, namely 50%/50%...
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[NMR paper] Probing the conformation of the sugar transport inhibitor phlorizin by 2D-NMR, molecu
Probing the conformation of the sugar transport inhibitor phlorizin by 2D-NMR, molecular dynamics studies, and pharmacophore analysis.
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J Med Chem. 2000 May 4;43(9):1692-8
Authors: Wielert-Badt S, Lin JT, Lorenz M, Fritz S, Kinne RK
Sodium/D-glucose cotransport, one of the prototypes for sodium gradient-driven symport systems in kidney and intestine, is known to be inhibited by aromatic and...
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11-18-2010 09:15 PM
[NMR paper] High-resolution solution structure of the inhibitor-free catalytic fragment of human
High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Related Articles High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Biochemistry. 1998 Feb 10;37(6):1495-504
Authors: Moy FJ, Chanda PK, Cosmi S, Pisano MR, Urbano C, Wilhelm J, Powers R
The high-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase (MMP-1), a...
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[NMR paper] 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase:
15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
Biochemistry. 1996 Dec 17;35(50):16036-47
Authors: Stivers JT, Abeygunawardana C, Mildvan AS
The solution secondary...
Conformation of inhibitor-free HIV-1 protease derived from NMR spectroscopy in a weakly oriented solution.
Linear Mode
