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Structural basis of the intrasteric regulation of myosin light chain kinases.

Publication ,  Journal Article
Knighton, DR; Pearson, RB; Sowadski, JM; Means, AR; Ten Eyck, LF; Taylor, SS; Kemp, BE
Published in: Science
October 2, 1992

The smooth muscle myosin light chain kinase (smMLCK) catalytic core was modeled by using the crystallographic coordinates of the cyclic AMP-dependent protein kinase catalytic subunit (cAPK) and a bound pseudosubstrate inhibitor peptide, PKI(5-24). Despite only 30% identity in amino acid sequence, the MLCK sequence can be readily accommodated in this structure. With the exception of the short B-helix, all major elements of secondary structure in the core are very likely conserved. The active site of the modeled MLCK complements the known requirements for peptide substrate recognition. MLCK contains a pseudosubstrate sequence that overlaps the calmodulin binding domain and has been proposed to act as an intrasteric inhibitor and occupy the substrate binding site in the absence of Ca(2+)-calmodulin. The pseudosubstrate sequence can be modeled easily into the entire backbone of PKI(5-24). The results demonstrate that the intrasteric model for regulation of MLCK by intramolecular competitive inhibition is structurally plausible.

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Published In

Science

DOI

ISSN

0036-8075

Publication Date

October 2, 1992

Volume

258

Issue

5079

Start / End Page

130 / 135

Location

United States

Related Subject Headings

  • Sequence Homology
  • Sequence Alignment
  • Protein Kinases
  • Protein Binding
  • Peptides
  • Peptide Fragments
  • Oligopeptides
  • Myosin-Light-Chain Kinase
  • Molecular Structure
  • Molecular Sequence Data
 

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Knighton, D. R., Pearson, R. B., Sowadski, J. M., Means, A. R., Ten Eyck, L. F., Taylor, S. S., & Kemp, B. E. (1992). Structural basis of the intrasteric regulation of myosin light chain kinases. Science, 258(5079), 130–135. https://doi.org/10.1126/science.1439761
Knighton, D. R., R. B. Pearson, J. M. Sowadski, A. R. Means, L. F. Ten Eyck, S. S. Taylor, and B. E. Kemp. “Structural basis of the intrasteric regulation of myosin light chain kinases.Science 258, no. 5079 (October 2, 1992): 130–35. https://doi.org/10.1126/science.1439761.
Knighton DR, Pearson RB, Sowadski JM, Means AR, Ten Eyck LF, Taylor SS, et al. Structural basis of the intrasteric regulation of myosin light chain kinases. Science. 1992 Oct 2;258(5079):130–5.
Knighton, D. R., et al. “Structural basis of the intrasteric regulation of myosin light chain kinases.Science, vol. 258, no. 5079, Oct. 1992, pp. 130–35. Pubmed, doi:10.1126/science.1439761.
Knighton DR, Pearson RB, Sowadski JM, Means AR, Ten Eyck LF, Taylor SS, Kemp BE. Structural basis of the intrasteric regulation of myosin light chain kinases. Science. 1992 Oct 2;258(5079):130–135.
Journal cover image

Published In

Science

DOI

ISSN

0036-8075

Publication Date

October 2, 1992

Volume

258

Issue

5079

Start / End Page

130 / 135

Location

United States

Related Subject Headings

  • Sequence Homology
  • Sequence Alignment
  • Protein Kinases
  • Protein Binding
  • Peptides
  • Peptide Fragments
  • Oligopeptides
  • Myosin-Light-Chain Kinase
  • Molecular Structure
  • Molecular Sequence Data