DSpace university logo mark
Advanced Search
Japanese | English 

NAOSITE : Nagasaki University's Academic Output SITE > Faculty of Engineering > Articles in academic journal >

Novel Ca 2+ -independent carbohydrate recognition of the C-type lectins, SPL-1 and SPL-2, from the bivalve Saxidomus purpuratus

File Description SizeFormat
ProtSci28_766.pdf1.37 MBAdobe PDFView/Open
ProtSci28_766_Suppl.pdf319.78 kBAdobe PDFView/Open

Title: Novel Ca 2+ -independent carbohydrate recognition of the C-type lectins, SPL-1 and SPL-2, from the bivalve Saxidomus purpuratus
Authors: Unno, Hideaki / Itakura, Shuhei / Higuchi, Shuhei / Goda, Shuichiro / Yamaguchi, Kenichi / Hatakeyama, Tomomitsu
Issue Date: 22-Feb-2019
Publisher: The Protein Society
Citation: Protein Science, 28(4), pp.766-778; 2019
Abstract: Novel Ca 2+ -independent C-type lectins, SPL-1 and SPL-2, were purified from the bivalve Saxidomus purpuratus. They are composed of dimers with either identical (SPL-2 composed of two B-chains) or distinct (SPL-1 composed of A- and B-chains) polypeptide chains, and show affinity for N-acetylglucosamine (GlcNAc)- and N-acetylgalactosamine (GalNAc)-containing carbohydrates, but not for glucose or galactose. A database search for sequence similarity suggested that they belong to the C-type lectin family. X-ray crystallographic analysis revealed definite structural similarities between their subunits and the carbohydrate-recognition domain (CRD) of the C-type lectin family. Nevertheless, these lectins (especially SPL-2) showed Ca 2+ -independent binding affinity for GlcNAc and GalNAc. The crystal structure of SPL-2/GalNAc complex revealed that bound GalNAc was mainly recognized via its acetamido group through stacking interactions with Tyr and His residues and hydrogen bonds with Asp and Asn residues, while widely known carbohydrate-recognition motifs among the C-type CRD (the QPD [Gln-Pro-Asp] and EPN [Glu-Pro-Asn] sequences) are not involved in the binding of the carbohydrate. Carbohydrate-binding specificities of individual A- and B-chains were examined by glycan array analysis using recombinant lectins produced from Escherichia coli cells, where both subunits preferably bound oligosaccharides having terminal GlcNAc or GalNAc with α-glycosidic linkages with slightly different specificities.
Keywords: bivalve / carbohydrate / C‐type lectin / X‐ray crystallographic analysis
URI: http://hdl.handle.net/10069/38945
ISSN: 09618368
DOI: 10.1002/pro.3592
Rights: This is the peer reviewed version of the following article: Protein Science, 28(4), pp.766-778; 2019, which has been published in final form at http://dx.doi.org/10.1002/pro.3592. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/38945

All items in NAOSITE are protected by copyright, with all rights reserved.


Valid XHTML 1.0! Copyright © 2006-2015 Nagasaki University Library - Feedback Powerd by DSpace