3NBC

Clitocybe nebularis ricin B-like lectin (CNL) in complex with lactose, crystallized at pH 4.4

3NBC の概要

• エントリーDOI: 10.2210/pdb3nbc/pdb
• 関連するPDBエントリー: 3NBD 3NBE
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: Ricin B-like lectin, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: clitocybe nebularis ricin b-like lectin, lactose, sugar binding protein
• 由来する生物種: Clitocybe nebularis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32083.38

構造登録者

Renko, M.,Pohleven, J.,Sabotic, J.,Kos, J.,Turk, D. (登録日: 2010-06-03, 公開日: 2011-09-21, 最終更新日: 2024-04-03)

主引用文献

Pohleven, J.,Renko, M.,Magister, S.,Smith, D.F.,Kunzler, M.,Strukelj, B.,Turk, D.,Kos, J.,Sabotic, J.
Bivalent carbohydrate binding is required for biological activity of Clitocybe nebularis lectin (CNL), the N,N'-diacetyllactosediamine (GalNAc beta 1-4GlcNAc, LacdiNAc)-specific lectin from basidiomycete C. nebularis
J.Biol.Chem., 287:10602-10612, 2012

PubMed Abstract: Lectins are carbohydrate-binding proteins that exert their biological activity by binding to specific cell glycoreceptors. We have expressed CNL, a ricin B-like lectin from the basidiomycete Clitocybe nebularis in Escherichia coli. The recombinant lectin, rCNL, agglutinates human blood group A erythrocytes and is specific for the unique glycan N,N'-diacetyllactosediamine (GalNAcβ1-4GlcNAc, LacdiNAc) as demonstrated by glycan microarray analysis. We here describe the crystal structures of rCNL in complex with lactose and LacdiNAc, defining its interactions with the sugars. CNL is a homodimeric lectin, each of whose monomers consist of a single ricin B lectin domain with its β-trefoil fold and one carbohydrate-binding site. To study the mode of CNL action, a nonsugar-binding mutant and nondimerizing monovalent CNL mutants that retain carbohydrate-binding activity were prepared. rCNL and the mutants were examined for their biological activities against Jurkat human leukemic T cells and the hypersensitive nematode Caenorhabditis elegans mutant strain pmk-1. rCNL was toxic against both, although the mutants were inactive. Thus, the bivalent carbohydrate-binding property of homodimeric CNL is essential for its activity, providing one of the rare pieces of evidence that certain activities of lectins are associated with their multivalency.

PubMed: 22298779
DOI: 10.1074/jbc.M111.317263

実験手法

X-RAY DIFFRACTION (1.01 Å)