1hlc: Difference between revisions
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[[Image:1hlc.gif|left|200px]] | [[Image:1hlc.gif|left|200px]] | ||
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1hlc |SIZE=350|CAPTION= <scene name='initialview01'>1hlc</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HLC is a [ | 1HLC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLC OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8262940 8262940] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:36 2008'' |
Revision as of 12:38, 20 March 2008
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, resolution 2.9Å | |||||||
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Gene: | CDNA (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[150571]
About this StructureAbout this Structure
1HLC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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