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Identification of protein oligomerization states by analysis of interface conservation
Journal article   Open access   Peer reviewed

Identification of protein oligomerization states by analysis of interface conservation

Adrian H Elcock and J. Andrew Mccammon
Proceedings of the National Academy of Sciences - PNAS, Vol.98(6), pp.2990-2994
03/06/2001
DOI: 10.1073/pnas.061411798
PMCID: PMC30594
PMID: 11248019
url
https://doi.org/10.1073/pnas.061411798View
Published (Version of record) Open Access

Abstract

The discrimination of true oligomeric protein–protein contacts from nonspecific crystal contacts remains problematic. Criteria that have been used previously base the assignment of oligomeric state on consideration of the area of the interface and/or the results of scoring functions based on statistical potentials. Both techniques have a high success rate but fail in more than 10% of cases. More importantly, the oligomeric states of several proteins are incorrectly assigned by both methods. Here we test the hypothesis that true oligomeric contacts should be identifiable on the basis of an increased degree of conservation of the residues involved in the interface. By quantifying the degree of conservation of the interface and comparing it with that of the remainder of the protein surface, we develop a new criterion that provides a highly effective complement to existing methods.
Biological Sciences

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