Rohrberg, J., Sachs, R., Lodderstedt, G., Sackewitz, M., Balbach, J. and Schwarz, E. (2008) Monitoring Fibril Formation of the N-Terminal Domain of PABPN1 Carrying an Alanine Repeat by Tryptophan Fluorescence and Real-Time NMR. FEBS Letters, 582, 1587-1592.
http://dx.doi.org/10.1016/j.febslet.2008.04.002

has been cited by the following article:

• TITLE: Gly→Ala Point Mutation and Conformation of Poly-Ala Stretch of PABPN1: A Molecular Dynamics Study

  AUTHORS: Mohd Shafique, Mohan Lal Garg, Fateh Singh Nandel

  KEYWORDS: Single Nucleotide Polymorphism, Gly→Ala Mutation, Poly-Ala, OPMD, PABPN1

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.6 No.2, May 5, 2015

  ABSTRACT: Single nucleotide replacing mutations in genes cause a number of diseases, but sometimes these mutations mimic other genetic mutations such as trinucleotide repeats expansions. A mutation in codon GGG→GCG results in Gly→Ala at the N-terminal of PABPN1 protein that mimics the trinucleotide repeat expansion disease called Oculopharyngeal muscular dystrophy (OPMD). Molecular dynamics simulations in water with peptide models having sequence Ac-A10-GA2GG-NHme (peptide A) and Ac-A10A3GG-NHme (peptide B) reveal an increase in the length of helical segment in peptide B. The α-helical length is found to be stable in peptide B with starting geometry of a right handed helix, while in the case peptide A, the helical length is short. The interactions of water molecules at terminals, side chain-backbone interactions and hydrogen bonds provide stability to resultant conformation. The adopted helix by the poly-Ala stretch may lead to masking some other active parts of the PABPN1 that may trigger the aggregation, decrease in degradation and/or impaired function of protein. Hence, further studies with N-terminal may be helpful to understand unclear disease mechanism.