2dur Citations

Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36.

J Biol Chem 282 28246-55 (2007)
Related entries: 2duo, 2dup, 2duq, 2e6v

Cited: 29 times
EuropePMC logo PMID: 17652092

Abstract

VIP36 functions as a transport lectin for trafficking certain high mannose type glycoproteins in the secretory pathway. Here we report the crystal structure of VIP36 exoplasmic/luminal domain comprising a carbohydrate recognition domain and a stalk domain. The structures of VIP36 in complex with Ca(2+) and mannosyl ligands are also described. The carbohydrate recognition domain is composed of a 17-stranded antiparallel beta-sandwich and binds one Ca(2+) adjoining the carbohydrate-binding site. The structure reveals that a coordinated Ca(2+) ion orients the side chains of Asp(131), Asn(166), and His(190) for carbohydrate binding. This result explains the Ca(2+)-dependent carbohydrate binding of this protein. The Man-alpha-1,2-Man-alpha-1,2-Man, which corresponds to the D1 arm of high mannose type glycan, is recognized by eight residues through extensive hydrogen bonds. The complex structures reveal the structural basis for high mannose type glycoprotein recognition by VIP36 in a Ca(2+)-dependent and D1 arm-specific manner.

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  1. Role of N-glycosylation in trafficking of apical membrane proteins in epithelia. Vagin O, Kraut JA, Sachs G. Am J Physiol Renal Physiol 296 F459-69 (2009)
  2. Survey of the year 2007 commercial optical biosensor literature. Rich RL, Myszka DG. J Mol Recognit 21 355-400 (2008)
  3. Role of Protein Glycosylation in Host-Pathogen Interaction. Lin B, Qing X, Liao J, Zhuo K. Cells 9 E1022 (2020)
  4. Convergent and divergent mechanisms of sugar recognition across kingdoms. Taylor ME, Drickamer K. Curr Opin Struct Biol 28 14-22 (2014)
  5. Man-Specific, GalNAc/T/Tn-Specific and Neu5Ac-Specific Seaweed Lectins as Glycan Probes for the SARS-CoV-2 (COVID-19) Coronavirus. Barre A, Damme EJMV, Simplicien M, Benoist H, Rougé P. Mar Drugs 18 E543 (2020)

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