Predicted structures of two proteins involved in human diseases |
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Authors: | Huan-Xiang Zhou Guoli Wang |
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Institution: | (1) Department of Physics, Drexel University, 19104 Philadelphia, PA |
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Abstract: | Structures of 79 proteins involved in human diseases were predicted by sequence alignments with structural templates. The
predicted structures for ALDP and CSA, proteins responsible for adrenoleukodystrophy and the Cockayne syndrome, respectively,
were analyzed to elucidate the molecular basis of disease mutations. In particular we positioned residue P484 of ALDP in the
homodimer interface. This positioning is consistent with a recent experimental finding that the mutation P484R significantly
decreases the self-interaction of ALDP and suggests that the disease mechanism of this mutation lies in the impaired ALDP
dimerization. We identified two new WD repeats in CSA and suggest that one of these forms part of the interaction surface
with other proteins. |
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Keywords: | Adrenoleukodystrophy the Cockayne syndrome disease mutation sequence alignment homology modeling |
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