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Protein Science, Vol 3, Issue 6 984-986, Copyright © 1994 by Cold Spring Harbor Laboratory Press
FOR THE RECORD |
E. E. HODGKIN, I. C. GILLMAN and R. J. GILBERT
British Bio-technology Limited, Watlington Road, Oxford OX4 5LY, United Kingdom
Secondary structure prediction of the catalytic domain of matrix metalloproteinases is evaluated in the light of recently published experimentally determined structures. The prediction was made by combining conformational propensity, surface probability, and residue conservation calculated for an alignment of 19 sequences. The position of each observed secondary structure element was correctly predicted with a high degree of accuracy, with a single {beta}-strand falsely predicted. The domain fold was also anticipated from the prediction by analogy with the structural elements found in the distantly related metalloproteinases thermolysin, astacin, and adamalysin.
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