1HLC

X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION

1HLC の概要

• エントリーDOI: 10.2210/pdb1hlc/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: HUMAN LECTIN, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: lectin
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29432.79

構造登録者

Lobsanov, Y.D.,Gitt, M.A.,Leffler, H.,Barondes, S.,Rini, J.M. (登録日: 1993-10-13, 公開日: 1994-04-30, 最終更新日: 2024-02-07)

主引用文献

Lobsanov, Y.D.,Gitt, M.A.,Leffler, H.,Barondes, S.H.,Rini, J.M.
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
J.Biol.Chem., 268:27034-27038, 1993

PubMed Abstract: S-Lac lectins are a family of soluble lactose-binding animal lectins, some of which have been implicated in modulating cell-cell and cell-matrix interactions through specific carbohydrate-mediated recognition. We report here the x-ray crystal structure of a representative member of this family, the human dimeric S-Lac lectin, L-14-II, in complex with lactose, at 2.9-A resolution. The two-fold symmetric dimer is made up of two extended anti-parallel beta-sheets, which associate in a beta-sandwich motif. Remarkably, the L-14-II monomer shares not only the same topology, but a very similar beta-sheet structure with that of the leguminous plant lectins, suggesting a conserved structure-function relationship. Carbohydrate binding by L-14-II was found to involve protein residues that are very highly conserved among all S-Lac lectins. These residues map to a single DNA exon, suggesting a carbohydrate binding cassette common to all S-Lac lectins.

PubMed: 8262940

実験手法

X-RAY DIFFRACTION (2.9 Å)