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1hlc

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[[Image:1hlc.gif|left|200px]]
[[Image:1hlc.gif|left|200px]]
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{{Structure
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|PDB= 1hlc |SIZE=350|CAPTION= <scene name='initialview01'>1hlc</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1hlc", creates the "Structure Box" on the page.
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|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1hlc| PDB=1hlc | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlc OCA], [http://www.ebi.ac.uk/pdbsum/1hlc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hlc RCSB]</span>
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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'''
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION'''
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[[Category: Lobsanov, Y D.]]
[[Category: Lobsanov, Y D.]]
[[Category: Rini, J M.]]
[[Category: Rini, J M.]]
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[[Category: lectin]]
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[[Category: Lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:58:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:10 2008''
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Revision as of 15:58, 2 May 2008

Template:STRUCTURE 1hlc

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


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.

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 Page seeded by OCA on Fri May 2 18:58:43 2008

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