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Advances in comparative protein-structure modelling

R Sánchez1, A Sali

  • 1Box 270, The Rockefeller University 1230 York Avenue, New York, NY 10021-6399, USA.

Current Opinion in Structural Biology
|April 1, 1997
PubMed
Summary
This summary is machine-generated.

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Comparative protein modelling accurately predicts 3D structures for many more sequences than experimentally determined ones. Despite some errors, this technique is increasingly useful for protein structure prediction.

Area of Science:

  • Structural biology
  • Bioinformatics
  • Computational chemistry

Background:

  • Experimental protein structure determination is limited.
  • Comparative modelling expands protein structure analysis to a larger sequence space.

Purpose of the Study:

  • To assess the accuracy and applications of comparative protein modelling.
  • To highlight the current limitations and growing utility of this computational method.

Main Methods:

  • Automated comparative modelling for protein sequences with >40% identity to known structures.
  • Analysis of error sources in comparative models.

Main Results:

  • Comparative modelling is applicable to ten times more sequences than experimental structures.

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  • Models achieve accuracy comparable to low-resolution X-ray or medium-resolution NMR structures.
  • Identified errors include side-chain packing, core segment/loop conformation, and sequence alignment.

    • Conclusions:

    • Comparative modelling is a powerful tool for protein structure prediction, despite current error sources.
    • The rapid growth in applications demonstrates its increasing value in structural biology and bioinformatics.