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Structural differences in the two major wheat germ agglutinin isolectins.

C S Wright, S Olafsdottir

The Journal of Biological Chemistry

|June 5, 1986

Summary

Structural differences between wheat germ agglutinin isolectin 1 (WGA1) and isolectin 2 (WGA2) were identified using X-ray diffraction and amino acid sequencing. Key variations in domain B suggest WGA1 has higher internal homology.

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Wheat germ agglutinin (WGA) is a lectin with multiple isolectins, including WGA1 and WGA2.
Understanding structural variations between WGA isolectins is crucial for elucidating their distinct biological functions.

Purpose of the Study:

To determine the structural differences between wheat germ agglutinin isolectin 1 (WGA1) and wheat germ agglutinin isolectin 2 (WGA2).
To correlate amino acid sequence variations with observed structural differences.

Main Methods:

X-ray diffraction analysis at 2.2 A resolution to compute electron density difference maps.
Amino acid sequencing of tryptic and thermolytic peptides of WGA1.
Fluorescence studies on tryptic peptide T-3.

Main Results:

The largest structural differences between WGA1 and WGA2 are localized in domain B.
Amino acid sequence analysis revealed four variable positions, three within domain B (His59Gln, His66Tyr, Pro56Thr) and one in domain C (Ser93Ala).
WGA1 exhibits a slightly higher degree of internal homology compared to WGA2.

Conclusions:

Specific amino acid substitutions in WGA1 account for its structural divergence from WGA2.
These substitutions, particularly in domain B, influence the overall structural characteristics and internal homology of WGA1.
Confirmation of a second tryptophan residue in WGA supports high-resolution structural data.

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