Abstract
Tandem repeats occur in 14% of all proteins. The repeat unit lengths range from a single amino acid to more than 100 residues and the repeat number is sometimes over 100. Understanding the structures, functions, and evolution of these repeats is a significant goal in both proteomics and genomics. This review summarizes experimental studies addressing structural features of tandem repeats of short oligopeptides that are rich in proline, glycine, asparagine, serine, and/or threonine. The oligopetides include (PGMG) and (PNN) in biomineralization protein (PM27), and (NPNA) in Plasmodium falciparum circumsporozoite protein, (YSPTSPS) in RNA polymerase II, (PHGGGWGQ) in the prion protein, (YGHGGG(N)) and (YNHGGG(G)) in plant glycine-rich proteins, (PGQGQQ), (PGQGQQGQQ) and (GYYPTSOQQ) of wheat HMW glutenin, (FGGMGGGKGG) in Aequipecten abductin. Spectroscopic studies including NMR and CD indicate that these peptides adopt type I and II β-turns, polyproline II helices, loop conformations, and random coils. Formation of these structures frequently depends on pH, solvent, temperature and hydration. The loop conformations are sometimes stabilized by cation-π, CH-π, and/or amino-aromatic interactions. These observations indicate that many tandem repeats are largely flexible. In addition to generating repeating domains and providing flexible linkers between domains, the tandem repeats of (PHGGGWGQ), (YGHGGG(N)) and (YNHGGG(G)) and those in titin bind Cu ions; whereas, tandem repeats of (NPNA) and those in elastin bind Ca ions. The interactions of some tandem repeats with various target proteins probably involve an induced fit. The tandem repeats in tropoelastin, flagelliform silk, wheat HMW glutenin, abductin, titin, and human nucleoporin, nup153, are responsible for elastomeric properties.
Keywords: Tandem repeat, proline, glycine, β-turn, polyproline II helix, flexible, elasticity, metal binding, intrinsically unstructured proteins
Current Protein & Peptide Science
Title: Flexible Structures and Ligand Interactions of Tandem Repeats Consisting of Proline, Glycine, Asparagine, Serine, and/or Threonine Rich Oligopeptides in Proteins
Volume: 9 Issue: 6
Author(s): Norio Matsushima, Hitoshi Yoshida, Yasuhiro Kumaki, Masakatsu Kamiya, Takanori Tanaka, Yoshinobu Izumi and Robert H. Kretsinger
Affiliation:
Keywords: Tandem repeat, proline, glycine, β-turn, polyproline II helix, flexible, elasticity, metal binding, intrinsically unstructured proteins
Abstract: Tandem repeats occur in 14% of all proteins. The repeat unit lengths range from a single amino acid to more than 100 residues and the repeat number is sometimes over 100. Understanding the structures, functions, and evolution of these repeats is a significant goal in both proteomics and genomics. This review summarizes experimental studies addressing structural features of tandem repeats of short oligopeptides that are rich in proline, glycine, asparagine, serine, and/or threonine. The oligopetides include (PGMG) and (PNN) in biomineralization protein (PM27), and (NPNA) in Plasmodium falciparum circumsporozoite protein, (YSPTSPS) in RNA polymerase II, (PHGGGWGQ) in the prion protein, (YGHGGG(N)) and (YNHGGG(G)) in plant glycine-rich proteins, (PGQGQQ), (PGQGQQGQQ) and (GYYPTSOQQ) of wheat HMW glutenin, (FGGMGGGKGG) in Aequipecten abductin. Spectroscopic studies including NMR and CD indicate that these peptides adopt type I and II β-turns, polyproline II helices, loop conformations, and random coils. Formation of these structures frequently depends on pH, solvent, temperature and hydration. The loop conformations are sometimes stabilized by cation-π, CH-π, and/or amino-aromatic interactions. These observations indicate that many tandem repeats are largely flexible. In addition to generating repeating domains and providing flexible linkers between domains, the tandem repeats of (PHGGGWGQ), (YGHGGG(N)) and (YNHGGG(G)) and those in titin bind Cu ions; whereas, tandem repeats of (NPNA) and those in elastin bind Ca ions. The interactions of some tandem repeats with various target proteins probably involve an induced fit. The tandem repeats in tropoelastin, flagelliform silk, wheat HMW glutenin, abductin, titin, and human nucleoporin, nup153, are responsible for elastomeric properties.
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Matsushima Norio, Yoshida Hitoshi, Kumaki Yasuhiro, Kamiya Masakatsu, Tanaka Takanori, Izumi Yoshinobu and Kretsinger H. Robert, Flexible Structures and Ligand Interactions of Tandem Repeats Consisting of Proline, Glycine, Asparagine, Serine, and/or Threonine Rich Oligopeptides in Proteins, Current Protein & Peptide Science 2008; 9 (6) . https://dx.doi.org/10.2174/138920308786733886
DOI https://dx.doi.org/10.2174/138920308786733886 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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