We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Inverse sequence similarity of proteins does not imply structural similarity
- Authors
Lorenzen, Stephan; Gille, Christoph; Preissner, Robert; Frömmel, Cornelius
- Abstract
There is a debate on the folding of proteins with inverted sequences. Theoretical approaches and experiments give contradictory results. Many proteins in the Protein Data Bank (PDB) show conspicuous inverse sequence similarity (ISS) to each other. Here we analyze whether this ISS is related to structural similarity. For the first time, we performed a large scale three-dimensional (3-D) superposition of corresponding Cα atoms of forwardly and inversely aligned proteins and tested the degree of secondary structure identity between them. Comparing proteins of less than 50% pairwise sequence identity, only 0.5% of the inversely aligned pairs had similar folds (99 out of 19 073), whereas about 9% of forwardly aligned proteins in the same score and length range show similar 3-D structures (1731 out of 19 248). This observation strongly supports the view that the inversion of sequences in almost all cases leads to a different folding property of the protein. Inverted sequences are thus suitable as protein-like sequences for control purposes without relations to existing proteins.
- Subjects
PROTEIN analysis; BIOMOLECULES
- Publication
FEBS Letters, 2003, Vol 545, Issue 2/3, p105
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)00450-2