1hlc
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(New page: 200px<br /> <applet load="1hlc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlc, resolution 2.9Å" /> '''X-RAY CRYSTAL STRUCT...)
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Revision as of 15:13, 12 November 2007
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X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION
Contents |
Overview
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.
Disease
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[150571]
About this Structure
1HLC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution., Lobsanov YD, Gitt MA, Leffler H, Barondes SH, Rini JM, J Biol Chem. 1993 Dec 25;268(36):27034-8. PMID:8262940
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