| 1. |
- Grahn, Elin M., 1970-, et al.
(författare)
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Structural Characterization of a Lectin from the Mushroom Marasmius oreades in Complex with the Blood Group B Trisaccharide and Calcium
- 2009
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Ingår i: Journal of Molecular Biology. - Amsterdam : Academic Press. - 0022-2836 .- 1089-8638. ; 390:3, s. 457-466
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Tidskriftsartikel (refereegranskat)abstract
- MOA (Marasmius oreades agglutinin), a lectin isolated from fruiting bodies of the mushroom M. oreades, specifically binds nonreducing terminal Galα(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galα(1,3)Galβ(1,4)GlcNAc and the branched blood group B determinant Galα(1,3)[Fucα(1,2)]Gal. Here, we present the crystal structure of MOA in complex with the blood group B trisaccharide solved at 1.8 Å resolution. To our knowledge, this is the first blood-group-B-specific structure reported in complex with a blood group B determinant. The carbohydrate ligand binds to all three binding sites of the N-terminal β-trefoil domain. Also, in this work, Ca2+ was included in the crystals, and binding of Ca2+ to the MOA homodimer altered the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.
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| 2. |
- Oresic, Matej, 1967-, et al.
(författare)
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Specific correlations between relative synonymous codon usage and protein secondary structure
- 1998
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Ingår i: Journal of Molecular Biology. - : Academic Press. - 0022-2836 .- 1089-8638. ; 281:1, s. 31-48
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Tidskriftsartikel (refereegranskat)abstract
- We found significant species-specific correlations between the use of two synonymous codons and protein secondary structure units by comparing the three-dimensional structures of human and Escherichia coli proteins with their mRNA sequences. The correlations are not explained by codon-context, expression level, GC/AU content, or positional effects. The E. coli correlation is between Asn AAC and the C-terminal regions of beta-sheet segments; it may result from selection for translational accuracy, suggesting the hypothesis that downstream Asn residues are important for beta-sheet formation. The correlation in human proteins is between Asp GAU and the N termini of alpha-helices; it may be important for eukaryote-specific sequential, cotranslational folding. The kingdom-specific correlations may reflect kingdom-specific differences in translational mechanisms. The correlations may help identify residues that are important for secondary structure formation, be useful in secondary structure prediction algorithms, and have implications for recombinant gene expression.
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