2rq8 › Citations

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.

Yagawa K, Yamano K, Oguro T, Maeda M, Sato T, Momose T, Kawano S, Endo T
Protein Sci 19 693-702 (2010)
Cited: 13 times
EuropePMC logo PMID: 20095049

Abstract

Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of I27, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects on protein stability during denaturant-induced "global unfolding" versus "vectorial unfolding" by mechanical pulling force or cellular unfolding systems. Here, we assessed the reason for the different effects of the Y9P mutation of I27 on the overall molecular stability and N-terminal unraveling by NMR. We found that the Y9P mutation causes a conformational change that is transmitted through beta-sheet structures to reach the central hydrophobic core in the interior and alters its accessibility to bulk solvent, which leads to destabilization of the hydrophobic core. On the other hand, the Y9P mutation causes a bend in the backbone structure, which leads to the formation of a more stable N-terminal structure probably through enhanced hydrophobic interactions.

Articles - 2rq8 mentioned but not cited (1)

  1. Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding. Yagawa K, Yamano K, Oguro T, Maeda M, Sato T, Momose T, Kawano S, Endo T. Protein Sci 19 693-702 (2010)


Reviews citing this publication (1)

  1. Structure of giant muscle proteins. Meyer LC, Wright NT. Front Physiol 4 368 (2013)

Articles citing this publication (11)

  1. Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences. Backes S, Hess S, Boos F, Woellhaf MW, Gödel S, Jung M, Mühlhaus T, Herrmann JM. J Cell Biol 217 1369-1382 (2018)
  2. Folding pathway of an Ig domain is conserved on and off the ribosome. Tian P, Steward A, Kudva R, Su T, Shilling PJ, Nickson AA, Hollins JJ, Beckmann R, von Heijne G, Clarke J, Best RB. Proc Natl Acad Sci U S A 115 E11284-E11293 (2018)
  3. Mimicking Ribosomal Unfolding of RNA Pseudoknot in a Protein Channel. Zhang X, Xu X, Yang Z, Burcke AJ, Gates KS, Chen SJ, Gu LQ. J Am Chem Soc 137 15742-15752 (2015)
  4. Computational modelling approaches as a potential platform to understand the molecular genetics association between Parkinson's and Gaucher diseases. Thirumal Kumar D, Eldous HG, Mahgoub ZA, George Priya Doss C, Zayed H. Metab Brain Dis 33 1835-1847 (2018)
  5. Detection of Internal Matrix Targeting Signal-like Sequences (iMTS-Ls) in Mitochondrial Precursor Proteins Using the TargetP Prediction Tool. Boos F, Mühlhaus T, Herrmann JM. Bio Protoc 8 e2474 (2018)
  6. Fuzzy oil drop model to interpret the structure of antifreeze proteins and their mutants. Banach M, Prymula K, Jurkowski W, Konieczny L, Roterman I. J Mol Model 18 229-237 (2012)
  7. Computational approach to unravel the impact of missense mutations of proteins (D2HGDH and IDH2) causing D-2-hydroxyglutaric aciduria 2. Thirumal Kumar D, Jerushah Emerald L, George Priya Doss C, Sneha P, Siva R, Charles Emmanuel Jebaraj W, Zayed H. Metab Brain Dis 33 1699-1710 (2018)
  8. Bioinformatics classification of mutations in patients with Mucopolysaccharidosis IIIA. Tanwar H, Kumar DT, Doss CGP, Zayed H. Metab Brain Dis 34 1577-1594 (2019)
  9. The Y9P Variant of the Titin I27 Module: Structural Determinants of Its Revisited Nanomechanics. Oroz J, Bruix M, Laurents DV, Galera-Prat A, Schönfelder J, Cañada FJ, Carrión-Vázquez M. Structure 24 606-616 (2016)
  10. Conformational stability of CopC and roles of residues Tyr79 and Trp83. Song Z, Zheng X, Yang B. Protein Sci 22 1519-1530 (2013)
  11. Prediction of folding mechanisms for Ig-like beta sandwich proteins based on inter-residue average distance statistics methods. Aumpuchin P, Kikuchi T. Proteins 87 120-135 (2019)


Quick links