Evolution of the multidomain protein wheat germ agglutinin Export

@article{Wright1985, abstract = {Summary We compared the homologous amino acid sequences of hevein and each of the four domains (A, B, C, and D) of wheat germ agglutinin and used them to construct a pseudophylogenetic tree relating these sequences to a hypothetical common ancestor sequence. In the crystal structure of the wheat germ agglutinin dimer, six pseudo-twofold rotational symmetry axes have previously been located in addition to the true twofold axis. Four of these relate two nonidentical domains to each other in each of the four possible pairs constituting the sugar-binding sites (A1D2, A2D1, B1C2, and B2C1). The remaining two relate contiguous unique pairs of sugar-binding sites to each other (A1D2 to B1C2, and A2D1 to B2C1). These latter two sets of pairs are related to each other by the true twofold axis. Side chains that mediate sugar binding in the interfaces of each of the four pairs were found to be largely conserved. The sequence homology, taken together with these pseudo-symmetry elements in the dimer structure, suggests a pathway for the evolution of the four-domain molecule from a single-domain dimer that can be correlated with simultaneous development of the saccharide-binding sites.}, author = {Wright, Tonie H. and Brooks, Danny M. and Wright, Christine S.}, citeulike-article-id = {4214623}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/BF02100087}, citeulike-linkout-1 = {http://www.springerlink.com/content/kt5700l406w55023}, day = {1}, doi = {10.1007/BF02100087}, journal = {Journal of Molecular Evolution}, keywords = {chitin-binding, duplication, evolution, triticum}, month = {February}, number = {2}, pages = {133--138}, posted-at = {2009-03-24 15:05:23}, priority = {2}, title = {Evolution of the multidomain protein wheat germ agglutinin}, url = {http://dx.doi.org/10.1007/BF02100087}, volume = {21}, year = {1985} }

TY - JOUR ID - Wright1985 L3 - citeulike-article-id:4214623 N2 - Summary We compared the homologous amino acid sequences of hevein and each of the four domains (A, B, C, and D) of wheat germ agglutinin and used them to construct a pseudophylogenetic tree relating these sequences to a hypothetical common ancestor sequence. In the crystal structure of the wheat germ agglutinin dimer, six pseudo-twofold rotational symmetry axes have previously been located in addition to the true twofold axis. Four of these relate two nonidentical domains to each other in each of the four possible pairs constituting the sugar-binding sites (A1D2, A2D1, B1C2, and B2C1). The remaining two relate contiguous unique pairs of sugar-binding sites to each other (A1D2 to B1C2, and A2D1 to B2C1). These latter two sets of pairs are related to each other by the true twofold axis. Side chains that mediate sugar binding in the interfaces of each of the four pairs were found to be largely conserved. The sequence homology, taken together with these pseudo-symmetry elements in the dimer structure, suggests a pathway for the evolution of the four-domain molecule from a single-domain dimer that can be correlated with simultaneous development of the saccharide-binding sites. IS - 2 JF - Journal of Molecular Evolution EP - 138 TI - Evolution of the multidomain protein wheat germ agglutinin VL - 21 SP - 133 KW - chitin-binding KW - duplication KW - evolution KW - triticum AU - Wright, Tonie AU - Brooks, Danny AU - Wright, Christine PY - 1985/02/01/ UR - http://dx.doi.org/10.1007/BF02100087 ER -