ArticleProtein science : a publication of the Protein Society1998
Effects of proline cis-trans isomerization on TB domain secondary structure.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Functional aspects of protein flexibility.Cellular and molecular life sciences : CMLS · 2009Review
- Computational structural analysis of an anti-L-amino acid antibody and inversion of its stereoselectivity.Journal of separation science · 2009Article
- Solution structure of a functionally active fragment of decay-accelerating factor.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Fibrillin: from microfibril assembly to biomechanical function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002Review
- The supramolecular organization of fibrillin-rich microfibrils.The Journal of cell biology · 2001Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The transforming growth factor beta (TGF-beta) binding protein-like (TB) domain is found principally in proteins localized to extracellular matrix fibrils, including human fibrillin-1, the defective protein in the Marfan syndrome. Analysis of the nuclear magnetic resonance (NMR) data for the sixth TB module from human fibrillin-1 has revealed the existence of two stable conformers that differ in the isomerization states of two proline residues. Unusually, the two isoforms do not readily interconvert and are stable on the time scale of milliseconds. We have computed independent structures of the major and minor conformers of TB6 to assess how the domain fold adjusts to incorporate alternatively cis- or trans-prolines. Based on previous observations, it has been suggested that multiple conformers can only be accommodated in flexible regions of protein structure. In contrast, P22, which exists in trans in the major form and cis in the minor form of TB6, is in a rigid region of the domain, which is confirmed by backbone dynamics measurements. Overall, the structures of the major and minor conformers are similar. However, the secondary structure topologies of the two forms differ as a direct consequence of the changes in proline conformation.
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