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Retrospective analysis of a secondary structure prediction: The catalytic domain of matrix metalloproteinases
Author(s) -
Hodgkin Edward E.,
Gillman Ian C.,
Gilbert Richard J.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030615
Subject(s) - thermolysin , matrix metalloproteinase , protein secondary structure , chemistry , biological system , crystallography , biology , biochemistry , enzyme , trypsin
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 β‐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.