Four-fold structural repeat in the acid proteases.

T L Blundell; B T Sewell; A D McLachlan

doi:10.1016/0005-2795(79)90194-6

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Four-fold structural repeat in the acid proteases.

T L Blundell·B T Sewell·A D McLachlan

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Abstract

The observation that the acid proteases contain two structurally equivalent lobes related by a dyad through the active centre has been extended to show that in endothiapepsin each lobe contains two similar halves related by a further local dyad. In lobe 1 22 pairs of alpha-carbons are equivalent with a root mean square deviation of 1.92 A. In lobe 2 17 pairs match within 2.31 A. Convergent evolution or gene quadruplication may have occurred.

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T L Blundell, B T Sewell, A D McLachlan. 1979-09-29. Four-fold structural repeat in the acid proteases.. https://doi.org/10.1016/0005-2795(79)90194-6

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