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An engineered retroviral proteinase from myeloblastosis associated virus acquires pH dependence and substrate specificity of the HIV-1 proteinase

Autor: Petr Štrop, J. Sedláček, Jan Konvalinka, Milan Fábry, I. Pichová, M Horejsí, S Foundling, Martin Andreánsky, P Novek, Ivo Bláha

Publikováno v: Scopus-Elsevier

In an attempt to understand the structural reasons for differences in specificity and activity of proteinases from two retroviruses encoded by human immunodeficiency virus (HIV) and myeloblastosis associated virus (MAV), we mutated five key residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d052921e799e5964277dd8dd29ceaa1e
https://doi.org/10.1002/j.1460-2075.1992.tb05154.x

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Isolation, biochemical characterization and crystallization of the p15gag proteinase of myeloblastosis associated virus expressed in E. coli

Autor: Vladimír Kostka, F. Kaprálek, Iva Pichová, Juraj Sedlacek, Vladimir Benes, S. Foundling, Petr Štrop, Milan Souček, L. Pavlíčková, M. Trávníček

Publikováno v: International Journal of Biochemistry. 24:235-242

1. 1. The p15 gag proteinase responsible for the processing of the polyprotein precursor of the myeloblastosis associated virus was obtained by a recombinant technique in an E. coli expression system. The massive expression of the intentionally trunc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32638250d961ee70c177e70030849e18
https://doi.org/10.1016/0020-711x(92)90252-v

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Intra- and intermolecular events direct the propeptide-mediated maturation of the Candida albicans secreted aspartic proteinase Sap1p

Autor: Utz Reichard, S. Foundling, S. Beggah, Michel Monod, Barbara Léchenne

Publikováno v: Microbiology (Reading, England). 146

Pathogenic yeasts of the genus Candida secrete aspartic proteinases (Sap) which are synthesized as preproenzymes. Expression of the C. albicans SAP1 gene lacking the propeptide-coding region in the methylotrophic yeast Pichia pastoris does not lead t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d222e874fb309a3377edf1b3330d2e33
https://pubmed.ncbi.nlm.nih.gov/11065355

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Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant

Autor: L, Hong, J A, Hartsuck, S, Foundling, J, Ermolieff, J, Tang

Publikováno v: Protein science : a publication of the Protein Society. 7(2)

The mutation Ala28 to serine in human immunodeficiency virus, type 1, (HIV-1) protease introduces putative hydrogen bonds to each active-site carboxyl group. These hydrogen bonds are ubiquitous in pepsin-like eukaryotic aspartic proteases. In order t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::82126da51b59ddbc70798ebe8af13c85
https://pubmed.ncbi.nlm.nih.gov/9521105

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Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs

Autor: L, Hong, X J, Zhang, S, Foundling, J A, Hartsuck, J, Tang

Publikováno v: FEBS letters. 420(1)

The crystal structure of human immunodeficiency virus type 1 (HIV-1) protease mutant G48H with peptidic inhibitor U-89360E is described. Comparison with wild-type protease-inhibitor complex shows that mutation of flap residue 48 to histidine allows s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6571ca2ea50c995686fa5423ed1dafd8
https://pubmed.ncbi.nlm.nih.gov/9450540

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The 2.8 A crystal structure of Gla-domainless activated protein C

Autor: V Oganessyan, Patrick R. Hof, Wolfram Bode, T. Mather, Robert Huber, Charles T. Esmon, S. Foundling

The structure of the Gla-domainless form of the human anticoagulant enzyme activated protein C has been solved at 2.8 A resolution. The light chain is composed of two domains: an epidermal growth factor (EGF)-like domain modified by a large insert co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd1c0b25fcb51c81f39dafbe78532915
https://europepmc.org/articles/PMC452507/

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Recombinant canditropsin, an extracellular aspartic protease from yeast Candida tropicalis. Escherichia coli expression, purification, zymogen activation, and enzymic properties

Autor: Jordan Tang, S. Foundling, Xinli Lin, Gerald Koelsch, M. Monod

Publikováno v: The Journal of biological chemistry. 268(27)

A cDNA fragment which encodes the zymogen of canditropsin, the extracellular aspartic protease from the yeast Candida tropicalis (Togni,G., Sanglard, D., Falchetto, R., and Monod, M. (1991) FEBS Lett. 286, 181-185) was cloned into a T7 expression vec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa651e37f363781bf2a4ad0cb8f26c2c
https://pubmed.ncbi.nlm.nih.gov/8376373

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Protein-Engineered Proteinase of Myeloblastosis Associated Virus, An Enzyme of High Activity and HIV-1 Proteinase-Like Specificity

Autor: Petr Štrop, Jan Konvalinka, M. Hořejší, Milan Fábry, Martin Andreánsky, Ivo Bláha, S. Foundling, L. Pavlíčková, Vladimír Kostka, J. Sedláček, I. Pichová, R. Škrabana, Jiří Velek, V. Černá

Publikováno v: Advances in Experimental Medicine and Biology ISBN: 9781468460148

All proteinases of avian and mammalian retroviruses belong to the family of aspartic proteinases, are of similar size and of homologous primary structure; they all act catalytically in the form of highly symmetric molecular dimers.1 Detailed studies

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fe7e03bb7d86107b4449f31a84f1982b
https://doi.org/10.1007/978-1-4684-6012-4_68

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