The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.
Open accessAbstract
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.
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Metadata
- Authors
- Lobsanov, Y. D., Gitt, M. A., Leffler, H., Barondes, S. H., & Rini, J. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-12
- Volume
- 268
- Issue
- 36
- Pages
- 27034-27038
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W4242509147
- Cited by
- 299
- References
- 30
- FWCI
- 7.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. https://app.cochat.ai/papers/10.1016/s0021-9258(19)74214-8
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- Lobsanov, Y. D., Gitt, M. A., Leffler, H., Barondes, S. H., & Rini, J. M. (1993). X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)74214-8
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