1hlc: Difference between revisions
New page: left|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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[[Image:1hlc.gif|left|200px]]<br /> | [[Image:1hlc.gif|left|200px]]<br /><applet load="1hlc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1hlc, resolution 2.9Å" /> | caption="1hlc, resolution 2.9Å" /> | ||
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION'''<br /> | '''X-RAY CRYSTAL STRUCTURE OF THE HUMAN DIMERIC S-LAC LECTIN, L-14-II, IN COMPLEX WITH LACTOSE AT 2.9 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
S-Lac lectins are a family of soluble lactose-binding animal lectins, some | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1HLC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1HLC is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barondes, S.]] | [[Category: Barondes, S.]] | ||
[[Category: Gitt, M | [[Category: Gitt, M A.]] | ||
[[Category: Leffler, H.]] | [[Category: Leffler, H.]] | ||
[[Category: Lobsanov, Y | [[Category: Lobsanov, Y D.]] | ||
[[Category: Rini, J | [[Category: Rini, J M.]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:26 2008'' | ||
Revision as of 14:02, 21 February 2008
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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
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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