[go: up one dir, main page]

Miura et al., 1999 - Google Patents

Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy …

Miura et al., 1999

View PDF
Document ID
2872155958664162846
Author
Miura T
Klaus W
Gsell B
Miyamoto C
Senn H
Publication year
Publication venue
Journal of molecular biology

External Links

Snippet

Ubiquitin-conjugating enzymes (Ubc) are involved in ubiquitination of proteins in the protein degradation pathway of eukaryotic cells. Ubc transfers the ubiquitin (Ub) molecules to target proteins by forming a thioester bond between their active site cysteine residue and the C …
Continue reading at www.academia.edu (PDF) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/1025—Acyltransferases (2.3)
    • C12N9/104—Aminoacyltransferases (2.3.2)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)

Similar Documents

Publication Publication Date Title
Miura et al. Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution
Terasawa et al. Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos
Wilkens et al. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
Arcus et al. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding
Pellecchia et al. NMR Structure of the J-domain and the Gly/Phe-rich Region of theEscherichia coliDnaJ Chaperone
Hill et al. 1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ (1-78)
Metzler et al. Identification of the poly-L-proline-binding site on human profilin.
Clubb et al. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin
Girvin et al. Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1Fo ATP synthase
Gronenborn et al. Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy
Banky et al. Isoform-specific differences between the type Iα and IIα cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR
Urbani et al. The metal binding site of the hepatitis C virus NS3 protease: A spectroscopic investigation
Nagadoi et al. Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexiblesubdomain
Siegal et al. Solution structure of the C-terminal SH2 domain of the p85α regulatory subunit of phosphoinositide 3-kinase
Li et al. Characterization of dual substrate binding sites in the homodimeric structure of Escherichia coli mRNA interferase MazF
Gosser et al. The solution structure of Abl SH3, and its relationship to SH2 in the SH (32) construct
Prutzman et al. The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation
Swarbrick et al. The three-dimensional structure of the Nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius L
Wilkinson et al. The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3
Muskett et al. The Solution Structure of Bovine Ferricytochromeb5Determined Using Heteronuclear NMR Methods
Kobayashi et al. Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange
Yangmee et al. Motional effects on NMR structural data: comparison of spinach and Escherichia coli acyl carrier proteins
Rodrigues et al. Drosophila melanogaster frataxin: protein crystal and predicted solution structure with identification of the iron-binding regions
Schmiedeskamp et al. NMR chemical shift perturbation mapping of DNA binding by a zinc‐finger domain from the yeast transcription factor ADR1
Keniry et al. NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli