Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases

Jaap J. Beintema*, Jan M. van der Laan

*Corresponding author for this work

    Research output: Contribution to journalArticleAcademicpeer-review

    11 Citations (Scopus)

    Abstract

    There are 33 invariant amino acid positions out of 132 positions in 42 investigated sequences of ribonucleases from a number of mammalian species and a reptile (snapping turtle, Chelydra serpentina). These invariant residues are unequally distributed over 3 different parts of the molecule. The lobe of the S-protein part of the molecule, which lacks one disulfide bridge and has two shortened loops in turtle ribonuclease, has the lowest percentage of invariant residues, although the active-site residue His 119 is located in this part
    Original languageEnglish
    Pages (from-to)338-342
    Number of pages5
    JournalFEBS Letters
    Volume194
    Issue number2
    DOIs
    Publication statusPublished - 6-Jan-1986

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