Structural sequence evolution and computational modeling approaches of the complement system in leishmaniasis.

Prajakta Ingale, Ritika Kabra, Shailza Singh

Journal: Advances in protein chemistry and structural biology 2021;120():409-424

PMID: 32085887

Full Text on Elsevier Science View on PubMed

Abstract

The complement system is one of the first barriers and consists of well-balanced cascades of reactions which generates anaphylatoxins such as C5a and C3a. A G-protein coupled receptor C5a anaphylatoxin chemotactic receptor 1 (C5AR1, also known as CD88) is the receptor for C5a which is present on cells of myeloid origin. Owing to difficulty in obtaining crystal structures of GPCRs in either inactive or active state, accurate structural modeling is still highly desirable for the majority of GPCRs. In an attempt to dissect the conformational changes associated with GPCR activation, computational modeling approaches is being pursued in this paper along with the evolutionary divergence to deal with the structural variability.

Address: National Centre for Cell Science, NCCS Complex, SP Pune University Campus, Pune, Maharashtra, India.

DOI: 10.1016/bs.apcsb.2019.12.004

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MeSH Terms: Amino Acid Sequence, Humans, Leishmaniasis, Models, Molecular, Phylogeny, Protein Conformation, Receptor, Anaphylatoxin C5a, Sequence Alignment