Correlation between protein function and ligand binding profiles

Matthew D. Shortridge, Michael Bokemper, Jennifer C. Copeland, Jaime L. Stark, Robert Powers

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

We report that proteins with the same function bind the same set of small molecules from a standardized chemical library. This observation led to a quantifiable and rapidly adaptable method for protein functional analysis using experimentally derived ligand binding profiles. Ligand binding is measured using a high-throughput NMR ligand affinity screen with a structurally diverse chemical library. The method was demonstrated using a set of 19 proteins with a range of functions. A statistically significant similarity in ligand binding profiles was only observed between the two functionally identical albumins and between the five functionally similar amylases. This new approach is independent of sequence, structure, or evolutionary information and, therefore, extends our ability to analyze and functionally annotate novel genes.

Original languageEnglish (US)
Pages (from-to)2538-2545
Number of pages8
JournalJournal of proteome research
Volume10
Issue number5
DOIs
StatePublished - May 6 2011

Keywords

  • NMR ligand affinity screen
  • functional annotation
  • functional genomics
  • ligand binding
  • protein function

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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