Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex
Journal Article
·
· Biochemistry; (United States)
A general approach is illustrated for providing detailed structural information on large enzyme/inhibitor complexes using NMR spectroscopy. The method involves the use of isotopically labeled ligands to simplify two-dimensional NOE spectra of large molecular complexes by isotope-editing techniques. With this approach, the backbone and side-chain conformations (at the P/sub 2/ and P/sub 3/ sites) of a tightly bound inhibitor of porcine pepsin have bene determined. In addition, structural information on the active site of pepsin has been obtained. Due to the sequence homology between porcine pepsin and human renin, this structural information may prove useful for modeling renin/inhibitor complexes with the ultimate goal of designing more effective renin inhibitors. Moreover, this general approach can be applied to study other biological systems of interest such as other enzyme/inhibitor complexes, ligands bound to soluble receptors, and enzyme/substrate interactions.
- Research Organization:
- Abbott Labs., Abbott Park, IL (USA)
- OSTI ID:
- 6142267
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:22; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Amide proton exchange rates of a bound pepsin inhibitor determined by isotope-edited proton NMR experiments
Slow step after bond-breaking by porcine pepsin identified using solvent deuterium isotope effects
Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin
Journal Article
·
Wed Sep 30 00:00:00 EDT 1987
· Biochem. Biophys. Res. Commun.; (United States)
·
OSTI ID:5856966
Slow step after bond-breaking by porcine pepsin identified using solvent deuterium isotope effects
Journal Article
·
Mon Apr 15 00:00:00 EDT 1991
· Biochemical and Biophysical Research Communications; (USA)
·
OSTI ID:5583566
Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin
Journal Article
·
Fri Jun 17 00:00:00 EDT 2005
· Biochemical and Biophysical Research Communications
·
OSTI ID:20710812
Related Subjects
550501* -- Metabolism-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ACID PROTEINASES
AMINO ACID SEQUENCE
BARYONS
CARBON 13
CARBON ISOTOPES
COMPLEXES
DEUTERIUM COMPOUNDS
ELEMENTARY PARTICLES
ENZYME INHIBITORS
ENZYMES
EVEN-ODD NUCLEI
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
HYDROLASES
ISOTOPES
LIGANDS
LIGHT NUCLEI
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
OVERHAUSER EFFECT
PEPSIN
PEPTIDE HYDROLASES
PROTONS
RESONANCE
STABLE ISOTOPES
59 BASIC BIOLOGICAL SCIENCES
ACID PROTEINASES
AMINO ACID SEQUENCE
BARYONS
CARBON 13
CARBON ISOTOPES
COMPLEXES
DEUTERIUM COMPOUNDS
ELEMENTARY PARTICLES
ENZYME INHIBITORS
ENZYMES
EVEN-ODD NUCLEI
FERMIONS
HADRONS
HYDROGEN COMPOUNDS
HYDROLASES
ISOTOPES
LIGANDS
LIGHT NUCLEI
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
OVERHAUSER EFFECT
PEPSIN
PEPTIDE HYDROLASES
PROTONS
RESONANCE
STABLE ISOTOPES