PMID: 6407541Mar 1, 1983Paper

Amino acid sequence restriction in relation to proteolysis

Bioscience Reports
H Jörnvall, B Persson

Abstract

Distributions of amino acid residues in proteins show that proline is overrepresented in sequence positions following two basic residues ([Lys Arg]-[Lys Arg]), i.e. at sites similar to those susceptible to proteolytic cleavages of hormonal pro-forms. Conformational correlations further show that [Lys Arg]-[Lys Arg]-Pro sequences are often (8/11) not adjacent to elements of secondary structure, whereas the opposite applies to [Lys Arg]-[Lys Arg]-nonPro sequences (82/103 adjacent to elements of secondary structure). These distribution patterns from proteins in general also seem applicable in individual protein groups as demonstrated for some dehydrogenases. It appears possible that [Lys Arg]-[Lys Arg]-nonPro constitutes a restricted sequence in proteins, and that proline, in addition to elements of secondary structure, contributes a means of avoiding unacceptable proteolytic processings of proteins in general.

References

Mar 25, 1976·Journal of Molecular Biology·H EklundA Akeson
Jun 1, 1978·Computers and Biomedical Research, an International Journal·R S CrowR J Prineas
Jun 20, 1977·Biochemical and Biophysical Research Communications·J G Beeley
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Oct 1, 1980·The Journal of General Virology·Y BeckerB Fridlender
Jan 1, 1981·Annual Review of Biochemistry·K A WalshK Titani

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Citations

Nov 14, 2003·Bioorganic Chemistry·Ann Eisenberg ShinnarHyon Ju Park
May 11, 2011·The British Journal of Nutrition·Hilde AlmaasGerd E Vegarud
Aug 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·R ReichhartH Jörnvall
Jan 19, 2000·Proceedings of the National Academy of Sciences of the United States of America·B ArunachalamP Cresswell

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