Predicting protein function from structure: unique structural features of proteases.

Abstract:

:We have noted consistent structural similarities among unrelated proteases. In comparison with other proteins of similar size, proteases have smaller than average surface areas, smaller radii of gyration, and higher C(alpha) densities. These findings imply that proteases are, as a group, more tightly packed than other proteins. There are also notable differences in secondary structure content between these two groups of proteins: proteases have fewer helices and more loops. We speculate that both high packing density and low alpha-helical content coevolved in proteases to avoid autolysis. By using the structural parameters that seem to show some separation between proteases and nonproteases, a neural network has been trained to predict protease function with over 86% accuracy. Moreover, it is possible to identify proteases whose folds were not represented during training. Similar structural analyses may be useful for identifying other classes of proteins and may be of great utility for categorizing the flood of structures soon to flow from structural genomics initiatives.

authors

Stawiski EW,Baucom AE,Lohr SC,Gregoret LM

doi

10.1073/pnas.070548997

keywords:

subject

Has Abstract

pub_date

2000-04-11 00:00:00

pages

3954-8

issue

8

eissn

0027-8424

issn

1091-6490

pii

070548997

journal_volume

97

pub_type

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