Novel carbohydrate-recognition mode of the invertebrate C-type lectin SPL-1 from Saxidomus purpuratus revealed by the GlcNAc-complex crystal in the presence of Ca².

ABSTRACT: The C-type lectins SPL-1 and SPL-2 from the bivalve Saxidomus purpuratus are composed of A and B chains and of two B chains, respectively. They bind specific carbohydrates containing acetamido groups, such as N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc), in a Ca²⁺-independent manner. Unlike ordinary C-type lectins, which require Ca²⁺ ions for carbohydrate recognition, these lectins recognize specific carbohydrates mainly through interactions with the acetamido group without Ca²⁺ ions, even though Ca²⁺ enhances the binding affinity of these lectins, especially SPL-1. In the present study, the crystal structure of the SPL-1-GlcNAc complex in the presence of Ca²⁺ revealed that the binding of SPL-1 to GlcNAc is stabilize

SUBMITTER: Unno H 

PROVIDER: S-EPMC7278497 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature