2dup
From Proteopedia
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Crystal structure of VIP36 exoplasmic/lumenal domain, metal-free form
Overview
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.
About this Structure
2DUP is a Single protein structure of sequence from Canis lupus familiaris with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36., Satoh T, Cowieson NP, Hakamata W, Ideo H, Fukushima K, Kurihara M, Kato R, Yamashita K, Wakatsuki S, J Biol Chem. 2007 Sep 21;282(38):28246-55. Epub 2007 Jul 25. PMID:17652092
Page seeded by OCA on Wed Jan 23 12:31:09 2008
