1HLC

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

Summary for 1HLC

• Entry DOI: 10.2210/pdb1hlc/pdb
• Related PRD ID: PRD_900004
• Descriptor: HUMAN LECTIN, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: lectin
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 29432.79

Authors

Lobsanov, Y.D.,Gitt, M.A.,Leffler, H.,Barondes, S.,Rini, J.M. (deposition date: 1993-10-13, release date: 1994-04-30, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)