Function and structure of inherently disordered proteins

A. Keith Dunker, Israel Silman, Vladimir N. Uversky, Joel L. Sussman

Research output: Contribution to journalReview article

657 Citations (Scopus)

Abstract

The application of bioinformatics methodologies to proteins inherently lacking 3D structure has brought increased attention to these macromolecules. Here topics concerning these proteins are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into specific groups, their structural preferences, their half-lives in cells, their contributions to signaling diversity (via high contents of multiple-partner binding sites, post-translational modifications, and alternative splicing), their distinct functional repertoire compared to that of structured proteins, and their involvement in diseases.

Original languageEnglish (US)
Pages (from-to)756-764
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume18
Issue number6
DOIs
StatePublished - Dec 1 2008

Fingerprint

Proteins
Sexual Partners
Alternative Splicing
Post Translational Protein Processing
Computational Biology
Eukaryota
Amino Acid Sequence
Binding Sites

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Function and structure of inherently disordered proteins. / Dunker, A. Keith; Silman, Israel; Uversky, Vladimir N.; Sussman, Joel L.

In: Current Opinion in Structural Biology, Vol. 18, No. 6, 01.12.2008, p. 756-764.

Research output: Contribution to journalReview article

Dunker, A. Keith ; Silman, Israel ; Uversky, Vladimir N. ; Sussman, Joel L. / Function and structure of inherently disordered proteins. In: Current Opinion in Structural Biology. 2008 ; Vol. 18, No. 6. pp. 756-764.
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