Structural classification of thioredoxin-like fold proteins

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

Protein structure classification is necessary to comprehend the rapidly growing structural data for better understanding of protein evolution and sequence-structure-function relationships. Thioredoxins are important proteins that ubiquitously regulate cellular redox status and various other crucial functions. We define the thioredoxin-like fold using the structure consensus of thioredoxin homologs and consider all circular permutations of the fold. The search for thioredoxin-like fold proteins in the PDB database identified 723 protein domains. These domains are grouped into eleven evolutionary families based on combined sequence, structural, and functional evidence. Analysis of the protein-ligand structure complexes reveals two major active site locations for the thioredoxin-like proteins. Comparison to existing structure classifications reveals that our thioredoxin-like fold group is broader and more inclusive, unifying proteins from five SCOP folds, five CATH topologies and seven DALI domain dictionary globular folding topologies. Considering these structurally similar domains together sheds new light on the relationships between sequence, structure, function and evolution of thioredoxins.

Original languageEnglish (US)
Pages (from-to)376-388
Number of pages13
JournalProteins: Structure, Function and Genetics
Volume58
Issue number2
DOIs
StatePublished - Feb 1 2005

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Thioredoxins
Proteins
Topology
Glossaries
Oxidation-Reduction
Catalytic Domain
Databases
Ligands

Keywords

  • Active site location
  • Circular permutation
  • Fold definition
  • Homology
  • Structural analog
  • Structure-based multiple sequence alignment

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Structural classification of thioredoxin-like fold proteins. / Qi, Yuan; Grishin, Nick V.

In: Proteins: Structure, Function and Genetics, Vol. 58, No. 2, 01.02.2005, p. 376-388.

Research output: Contribution to journalArticle

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