Autor: Wlodawer, Alexander - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Structural studies of algal lectins with anti-HIV activity
Autorzy:: Ziółkowska, Natasza
Wlodawer, Alexander
Powiązania:: https://bibliotekanauki.pl/articles/1041149.pdf
Data publikacji:: 2006
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: topical antivirals
protein structure
HIV
lectin
AIDS
Opis:: A number of antiviral lectins, small proteins that bind carbohydrates found on viral envelopes, are currently in pre-clinical trials as potential drugs for prevention of transmission of human immunodeficiency virus (HIV) and other enveloped viruses, such as the Ebola virus and the coronavirus responsible for severe acute respiratory syndrome (SARS). Lectins of algal origin whose antiviral properties make them candidate agents for prevention of viral transmission through topical applications include cyanovirin-N, Microcystis viridis lectin, scytovirin, and griffithsin. Although all these proteins exhibit significant antiviral activity, their structures are unrelated and their mode of binding of carbohydrates differs significantly. This review summarizes the current state of knowledge of the structures of algal lectins, their mode of binding of carbohydrates, and their potential medical applications.
Źródło:: Acta Biochimica Polonica; 2006, 53, 4; 617-626
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

Artykuł

Skocz do pozycji: 2.

Tytuł:: Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Autorzy:: Wlodawer, Alexander
Li, Mi
Gustchina, Alla
Oyama, Hiroshi
Dunn, Ben
Oda3, Kohei
Powiązania:: https://bibliotekanauki.pl/articles/1043650.pdf
Data publikacji:: 2003
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: enzyme families
sequence conservation
active site
enzymatic machanism
protein structure
Opis:: Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus novo sp. MN-32. The availability of these crystal structures enabled us to model the structure of mammalian CLN2, an enzyme which, when mutated in humans, leads to a fatal neurodegenerative disease. This review compares the structural and enzymatic properties of this newly defined MEROPS family of peptidases, S53, and introduces their new nomenclature.
Źródło:: Acta Biochimica Polonica; 2003, 50, 1; 81-102
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

Artykuł

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