Structural differences in the two major wheat germ agglutinin isolectins.
作者： C S Wright , S Olafsdottir
DOI: 10.1016/S0021-9258(17)38373-4
关键词:
摘要: We have combined amino acid sequence data with x-ray diffraction results to determine differences in structure of wheat germ agglutinin isolectin 1 (WGA1) relative the known 2 (WGA2). Electron density difference maps computed at 2.2 A resolution coefficients [2F(WGA1) - F(WGA2)] and [F(WGA1) based on refined model phases WGA2 revealed that largest two structures are localized B-domain molecule. Amino studies tryptic thermolytic peptides WGA1 confirm strong homology between isolectins suggest variability only four positions. Three these closely spaced domain B. The histidines WGA2, His59 His66, substituted by Gln Tyr, respectively, Pro56, Thr WGA1. fourth position 93 C was identified as a change from Ser (WGA2) Ala (WGA1). With substitutions exhibits slightly higher degree internal than does WGA2. In addition, we carried out fluorescence peptide T-3 presence second Trp residue molecule, recently predicted 41 during course high crystal refinement
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