1hlc: Difference between revisions
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|PDB= 1hlc |SIZE=350|CAPTION= <scene name='initialview01'>1hlc</scene>, resolution 2.9Å | |PDB= 1hlc |SIZE=350|CAPTION= <scene name='initialview01'>1hlc</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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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==Overview== | ==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. | 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== | ==About this Structure== | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:10 2008'' | ||
