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Volumn 321, Issue 5897, 2008, Pages 1834-1837

Antigen recognition by variable lymphocyte receptors

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BLOOD GROUP H ANTIGEN; BLOOD GROUP O ANTIGEN; LYMPHOCYTE RECEPTOR; TRISACCHARIDE;

EID: 52949150063     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1162484     Document Type: Article
Times cited : (159)

References (34)
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    • When the distribution of LRRV modules per transcript was analyzed from 517 unique VLR sequences, VLRs were found to have an average of 1.31 LRRV modules between the canonical LRR1 and LRRVe modules (2): 109 VLRs (0 LRRV), 228 VLRs (1 LRRV), 119 VLRs (2 LRRVs), 45 VLRs (3 LRRVs), 6 VLRs (4 LRRVs), 8 VLRs (5 LRRVs), 1 VLR (6 LRRVs), and 1 VLR (7 LRRVs).
    • When the distribution of LRRV modules per transcript was analyzed from 517 unique VLR sequences, VLRs were found to have an average of 1.31 LRRV modules between the canonical LRR1 and LRRVe modules (2): 109 VLRs (0 LRRV), 228 VLRs (1 LRRV), 119 VLRs (2 LRRVs), 45 VLRs (3 LRRVs), 6 VLRs (4 LRRVs), 8 VLRs (5 LRRVs), 1 VLR (6 LRRVs), and 1 VLR (7 LRRVs).
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    • At least four subtypes of H-antigens are known, which can be further converted into the A-antigen of human blood group A and B-antigen of human blood group B by glycosyltransferases A and B, respectively 31, fig. S1
    • At least four subtypes of H-antigens are known, which can be further converted into the A-antigen of human blood group A and B-antigen of human blood group B by glycosyltransferases A and B, respectively (31) (fig. S1).
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    • Single-letter abbreviations for amino acid residues: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr.
    • Single-letter abbreviations for amino acid residues: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr.
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    • Aromatic residues, such as Trp and Tyr, are frequently observed in the protein sugar-binding sites. For example, in the maltose/maltooligosaccharide- binding protein (32), aromatic residues play a major role in carbohydrate recognition and binding by providing not only hydrophobic stacking interactions between aromatic residues and the hydrophobic face of the sugar rings, but also polar contacts to the sugar hydroxyl groups.
    • Aromatic residues, such as Trp and Tyr, are frequently observed in the protein sugar-binding sites. For example, in the maltose/maltooligosaccharide- binding protein (32), aromatic residues play a major role in carbohydrate recognition and binding by providing not only hydrophobic stacking interactions between aromatic residues and the hydrophobic face of the sugar rings, but also polar contacts to the sugar hydroxyl groups.
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    • We thank R. L. Stanfield, X. Dai, and X. Zhu for help with data collection and analysis; M. N. Alder for help with VLR cDNA library preparation; J. Paulson and R. McBride for helpful comments and suggestions; and J. Vanhnasy, B. Droese, and H.-J. Kim for technical support and advice. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory (SSRL, operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. Supported by NIH grants AI42266 (I.A.W, and AI072435 (M.D.C, the Georgia Research Alliance (M.D.C, and the Skaggs Institute for Chemical Biology (I.A.W, This is Scripps Research Institute manuscript 19581-MB. Coordinates and structure factors have been deposited in the Protein Data Bank (PDB) with accession code 3E6J
    • We thank R. L. Stanfield, X. Dai, and X. Zhu for help with data collection and analysis; M. N. Alder for help with VLR cDNA library preparation; J. Paulson and R. McBride for helpful comments and suggestions; and J. Vanhnasy, B. Droese, and H.-J. Kim for technical support and advice. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory (SSRL), operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences. Supported by NIH grants AI42266 (I.A.W.) and AI072435 (M.D.C.), the Georgia Research Alliance (M.D.C.), and the Skaggs Institute for Chemical Biology (I.A.W.). This is Scripps Research Institute manuscript 19581-MB. Coordinates and structure factors have been deposited in the Protein Data Bank (PDB) with accession code 3E6J.


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