F-type Lectin Domains: Provenance, Prevalence, Properties, Peculiarities, and Potential.

Mahajan, Sonal and Ramya, T N C (2018) F-type Lectin Domains: Provenance, Prevalence, Properties, Peculiarities, and Potential. Advances in experimental medicine and biology, 1112. pp. 345-363. ISSN 0065-2598

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Official URL: https://link.springer.com/chapter/10.1007%2F978-98...


F-type lectins are phylogenetically widespread albeit selectively distributed lectins with an L-fucose-binding sequence motif and an F-type lectin fold. Several F-type lectins from fishes have been extensively studied, and structural information is available for F-type lectin domains from fish and bacterial proteins. F-type lectins have been demonstrated to be involved in self-/nonself-recognition and therefore have an important role in pathogen defense in many metazoan animals. F-type lectin domains also have been implicated in functions related to fertilization, protoplast regeneration, and bacterial virulence. We have recently analyzed and reported the taxonomic spread, phylogenetic distribution, architectural contexts, and sequence characteristics of prokaryotic and eukaryotic F-type lectin domains. Interestingly, while eukaryotic F-type lectin domains were frequently present as stand-alone domains, bacterial F-type lectin domains were mostly found co-occurring with enzymatic or nonenzymatic domains in diverse domain architectures, suggesting that the F-type lectin domain might be involved in targeting enzyme activities or directing other biological functions to distinct glycosylated niches in bacteria. We and others have probed the fine oligosaccharide-binding specificity of several F-type lectin domains. The currently available wealth of sequence, structural, and biochemical information about F-type lectin domains provides opportunities for the generation of designer lectins with improved binding strength and altered binding specificities. We discuss the prevalence, provenance, properties, peculiarities, and potential of F-type lectin domains for future applications in this review.

Item Type: Article
Additional Information: Copyright of this article belongs to Springer Nature.
Uncontrolled Keywords: Domain architectures; F-type lectin domain; L-fucose; Motif; Structural features
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 20 Mar 2019 10:13
Last Modified: 20 Mar 2019 11:43
URI: http://crdd.osdd.net/open/id/eprint/2186

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