A
Alla Gustchina
Researcher at National Institutes of Health
Publications - 98
Citations - 3978
Alla Gustchina is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Protease & Proteases. The author has an hindex of 37, co-authored 93 publications receiving 3761 citations. Previous affiliations of Alla Gustchina include Brookhaven National Laboratory & Government of the United States of America.
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Journal ArticleDOI
Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma.
Alexander Zdanov,Céline Schalk-Hihi,Alla Gustchina,Monica Tsang,James Weatherbee,Alexander Wlodawer +5 more
TL;DR: The structure of IL-10 provides insights into the possible modes of conversion of the dimer into monomers, and of putative sites of receptor interactions, and shows that the internal disorder often associated with other helical cytokines is not an essential feature of this class of proteins.
Journal ArticleDOI
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.
Istvan Botos,E.E. Melnikov,Scott Cherry,Joseph E. Tropea,Anna G. Khalatova,Rasulova Fs,Zbigniew Dauter,Michael R. Maurizi,T. V. Rotanova,Alexander Wlodawer,Alla Gustchina +10 more
TL;DR: Alignment of the P domain catalytic pocket with those of several Ser-Lys dyad peptide hydrolases provides a model of substrate binding, suggesting that polypeptides are oriented in the Lon active site to allow nucleophilic attack by the serine hydroxyl on the si-face of the peptide bond.
Journal ArticleDOI
Structural and biochemical studies of retroviral proteases.
TL;DR: Structural and biochemical data for retroviral proteases are compared in order to analyze the similarities and differences between the enzymes from different sources and to enhance the understanding of their properties.
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Selectivity in the Inhibition of HIV and FIV Protease: Inhibitory and Mechanistic Studies of Pyrrolidine-Containing .alpha.-Keto Amide and Hydroxyethylamine Core Structures
Deborah H. Slee,Karen Laslo,John H. Elder,Ian R. Ollmann,Alla Gustchina,Jukka Kervinen,Alexander Zdanov,Alexander Wlodawer,Chi-Huey Wong +8 more
Journal ArticleDOI
Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution
TL;DR: The structure‐based alignment of IL‐4 and GM‐CSF revealed that the core of the molecules, including large parts of all four helices and extending over half of the molecule, has 30% sequence identity, which may have identified regions which are not only important to maintain structure, but could also play a role in receptor binding.