A5048742550- Enzyme Production and Characterization
- Enzyme Structure and Function
- HIV/AIDS drug development and treatment
- HIV Research and Treatment
- Malaria Research and Control
- Peptidase Inhibition and Analysis
- Monoclonal and Polyclonal Antibodies Research
- Bacterial Genetics and Biotechnology
- Allergic Rhinitis and Sensitization
- Biochemical and Structural Characterization
- Food Allergy and Anaphylaxis Research
- RNA and protein synthesis mechanisms
- Biochemical and Molecular Research
- Protein Structure and Dynamics
- Glycosylation and Glycoproteins Research
- Insects and Parasite Interactions
- Insect and Pesticide Research
- Immune Response and Inflammation
- Coagulation, Bradykinin, Polyphosphates, and Angioedema
- Protein Hydrolysis and Bioactive Peptides
- Viral Infectious Diseases and Gene Expression in Insects
- Chemical Synthesis and Analysis
- Click Chemistry and Applications
- Ubiquitin and proteasome pathways
- Cancer Research and Treatments
National Cancer Institute
2015-2024
Frederick National Laboratory for Cancer Research
2010-2021
Center for Cancer Research
2005-2021
Institute of Crystallography
2005-2020
Government of the United States of America
2020
National Institutes of Health
2003-2015
Institute of Experimental Cardiology
2008
Nagasaki University
2008
Cancer Research Center
1990-2006
Science Applications International Corporation (United States)
2005
AI-strand A-turn A,-strand B-loop: B1-strand B-turn Bz-strand BC-connecting region Cl-helical type fold
The crystal structure of human recombinant interleukin‐4 (IL‐4) has been solved by multiple isomorphous replacement, and refined to an R factor 0.218 at 2.25 Å resolution. molecule is a left‐handed four‐helix bundle with short stretch β sheet. bears close resemblance other cytokines such as granulocyte‐macrophage colony stimulating (GM‐CSF). Although no sequence similarity IL‐4 GM‐CSF related previously postulated, structure‐based alignment revealed that the core molecules, including large...
The sequence requirements for HIV-1 proteinase catalyzed cleavage of oligopeptides containing two distinct types junctions (-hydrophobic*hydrophobic- or -aromatic*Pro-) has been investigated. For the first type junction (-hydrophobic*hydrophobic-) optimal residues in P2 and P2' positions were found to be Val Glu, respectively, accord with recent statistical analysis natural sites [Poorman, R. A., Tomasselli, A. G., Heinrikson, L., & Kézdy, F. J. (1991) Biol. Chem. 266, 14554-14561]....
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSelectivity in the Inhibition of HIV and FIV Protease: Inhibitory Mechanistic Studies Pyrrolidine-Containing .alpha.-Keto Amide Hydroxyethylamine Core StructuresDeborah H. Slee, Karen L. Laslo, John Elder, Ian R. Ollmann, Alla Gustchina, Jukka Kervinen, Alexander Zdanov, Wlodawer, Chi-Huey WongCite this: J. Am. Chem. Soc. 1995, 117, 48, 11867–11878Publication Date (Print):December 1, 1995Publication History Published online1 May 2002Published...
ATP‐dependent Lon proteases belong to the superfamily of AAA + proteins. Until recently, identity residues involved in their proteolytic active sites was not elucidated. However, putative catalytic Ser–Lys dyad recently suggested through sequence comparison more than 100 from various sources. The presence experimentally confirmed by site‐directed mutagenesis Escherichia coli protease and determination crystal structure its domain. Furthermore, this extensive analysis allowed definition two...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTKinetic and modeling studies of S3-S3' subsites HIV proteinasesJozsef Tozser, Irene T. Weber, Alla Gustchina, Ivo Blaha, Terry D. Copeland, John M. Louis, Stephen OroszlanCite this: Biochemistry 1992, 31, 20, 4793–4800Publication Date (Print):May 1, 1992Publication History Published online1 May 2002Published inissue 1 1992https://pubs.acs.org/doi/10.1021/bi00135a008https://doi.org/10.1021/bi00135a008research-articleACS PublicationsRequest reuse...
The crystal structure of a 1:1 complex between the German cockroach allergen Bla g 2 and Fab' fragment monoclonal antibody 7C11 was solved at 2.8-angstroms resolution. binds to through four loops that include residues 60-70, 83-86, 98-100, 129-132. Cation-pi interactions exist Lys-65, Arg-83, Lys-132 in several tyrosines 7C11. In with Fab', forms dimer, which is stabilized by quasi-four-helix bundle comprised an alpha-helix helical turn from each monomer, exhibiting novel dimerization mode...
Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features these a unique triad, Ser-Glu-Asp, as well presence an aspartic acid residue in oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, kumamolisin thermophilic bacterium, Bacillus novo MN-32....
The crystal structure of HIV‐1 protease with an inhibitor has been compared the structures non‐viral aspartic proteases complexed inhibitors. In dimeric protease, two 4‐stranded β‐sheets are formed by half inhibitor, residues 27–29, and flap from each monomer. monomeric enzyme single does not form a β‐sheet inhibitor. shows more interactions longer peptide than observed in protease‐inhibitor complexes. This, large movement flaps, restricts conformation cleavage sites retroviral polyprotein precursor.
Kinetic analysis of the hydrolysis peptide H‐Vat‐Ser‐Gin‐Asn‐Tyr*Pro‐He‐Val‐Gin‐NH 2 and its analogs obtained by varying length introducing substitutions at P 4 site was carried out with both HIV‐1 HIV‐2 proteinases. Deletion terminal Val Gin had only moderate effect on substrate hydrolysis, while deletion , Ser as well 3 greatly reduced hydrolysis. This is predicted to be due loss interactions between main chains enzyme substrate. Substitution amino acids having a high frequency occurrence...