Protein kinase superfamily - comparisons of sequence data with three-dimensional structures

Lei Wei, Stevan R. Hubbard, Randall F. Smith, Leland Ellis

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The elucidation of the three-dimensional structures of complexes of the catalytic subunit of mouse recombinant CAMP-dependent protein kinase with bound divalent ion, nucleotide and peptide inhibitor provides new insights into the structural organization of the active site of this enzyme and the probable roles of individual residues in catalysis. Further, the structure of a second member of the eukaryotic kinase superfamily, human cyclin-dependent kinase 2, now provides a first look at both the similarities and the variations in kinase structure.

Original languageEnglish (US)
Pages (from-to)450-455
Number of pages6
JournalCurrent Opinion in Structural Biology
Volume4
Issue number3
DOIs
StatePublished - 1994
Externally publishedYes

Fingerprint

Protein Kinases
Catalytic Domain
Phosphotransferases
Catalysis
Nucleotides
Ions
Peptides
Enzymes
human CDK2 protein

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Protein kinase superfamily - comparisons of sequence data with three-dimensional structures. / Wei, Lei; Hubbard, Stevan R.; Smith, Randall F.; Ellis, Leland.

In: Current Opinion in Structural Biology, Vol. 4, No. 3, 1994, p. 450-455.

Research output: Contribution to journalArticle

Wei, Lei ; Hubbard, Stevan R. ; Smith, Randall F. ; Ellis, Leland. / Protein kinase superfamily - comparisons of sequence data with three-dimensional structures. In: Current Opinion in Structural Biology. 1994 ; Vol. 4, No. 3. pp. 450-455.
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