Comparing sequence and structure of falcipains and human homologs at prodomain and catalytic active site for malarial peptide-based inhibitor design:

Musyoka, Thommas M; Njuguna, Joyce N; Tastan Bishop, Özlem

Title: Comparing sequence and structure of falcipains and human homologs at prodomain and catalytic active site for malarial peptide-based inhibitor design:
Creator: Musyoka, Thommas M, Njuguna, Joyce N, Tastan Bishop, Özlem
Date: 2018
Type: text
Type: article
Identifier: http://hdl.handle.net/10962/148392
Identifier: vital:38735
Identifier: DOI: 10.1101/381566
Description: Falcipains are major cysteine proteases of Plasmodium falciparum involved in haemoglobin degradation and remain attractive anti-malarial drug targets. Several inhibitors against these proteases have been identified, yet none of them has been approved for malaria treatment. Other Plasmodium species also possess highly homologous proteins to falcipains. For selective therapeutic targeting, identification of sequence and structure differences with homologous human cathepsins is necessary. The substrate processing activity of these proteins is tightly controlled via a prodomain segment occluding the active site which is chopped under low pH conditions exposing the catalytic site. Current work characterizes these proteases to identify residues mediating the prodomain regulatory function for the design of peptide based anti-malarial inhibitors.
Format: pdf
Language: English
Relation: Malaria journal, Musyoka, T.M., Njuguna, J.N. and Bishop, Ö.T., 2019. Comparing sequence and structure of falcipains and human homologs at prodomain and catalytic active site for malarial peptide based inhibitor design. Malaria journal, 18(1), p.159., Malaria journal volume 18 number 1 p.159 2018 1475-2875
Rights: Publisher
Rights: Use of this resource is governed by the terms and conditions of the SpringerLink Terms of Use Statement ( https://link.springer.com/termsandconditions)

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Tastan Bishop, Ozlem (Prof)

RU Research Unit in Bioinformatics (RUBi)

RU Department of Biochemistry, Microbiology and Bioinformatics

SDG 03. Good Health and Well-Being

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