Abstract
In this work, we propose the identification of structural motifs in the C-terminal region of the Leishmania cysteine proteinase, a region that can characterize epitopes of human T cells, using molecular modeling calculations. Multiple sequence alignment and homology modeling were used to build a three-dimensional model structure for the cysteine proteinase. With this theoretical proposition of three-dimensional structure, three distinct regions can be assigned: α-helix regions (α1, 224–232 CFDKNCTQGC; α2, 240–253 ANECHKNGGGASM and α3, 257–272 SPQKVTMCTYSNEFCV), two small strain regions (214–216 PAP and 237–239 LIK) being the major part of the COOH-terminal region assigned as coils. The linear sequence of the COOH-terminal region of the cysteine proteinase of Leishmania allows at least three epitope regions, the structural motifs found corroborate this information and encourages our experimental studies.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
