scholarly journals The Homology Model of PMP22 Suggests Mutations Resulting in Peripheral Neuropathy Disrupt Transmembrane Helix Packing

Biochemistry ◽  
2014 ◽  
Vol 53 (39) ◽  
pp. 6139-6141 ◽  
Author(s):  
Kathleen F. Mittendorf ◽  
Brett M. Kroncke ◽  
Jens Meiler ◽  
Charles R. Sanders
Keyword(s):  
Peripheral Neuropathy ◽  
Transmembrane Helix ◽  
Homology Model ◽  
Helix Packing

scholarly journals Helix Packing in Polytopic Membrane Proteins: Role of Glycine in Transmembrane Helix Association

1999 ◽  
Vol 77 (3) ◽  
pp. 1609-1618 ◽  
Author(s):  
Maryam M. Javadpour ◽  
Markus Eilers ◽  
Michel Groesbeek ◽  
Steven O. Smith
Keyword(s):  
Membrane Proteins ◽  
Transmembrane Helix ◽  
Helix Packing

scholarly journals Robust Driving Forces for Transmembrane Helix Packing

2012 ◽  
Vol 103 (6) ◽  
pp. 1227-1235 ◽  
Author(s):  
Ayelet Benjamini ◽  
Berend Smit
Keyword(s):  
Driving Forces ◽  
Transmembrane Helix ◽  
Helix Packing

scholarly journals The role of hydrophobic matching on transmembrane helix packing in cells

Cell Stress ◽  
2017 ◽  
Vol 1 (2) ◽  
pp. 90-106 ◽  
Author(s):  
Brayan Grau ◽  
Matti Javanainen ◽  
Maria Jesús García-Murria ◽  
Waldemar Kulig ◽  
Ilpo Vattulainen ◽  
...  
Keyword(s):  
Transmembrane Helix ◽  
Helix Packing ◽  
Hydrophobic Matching ◽  
In Cells

scholarly journals Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hHV1

2013 ◽  
Vol 142 (6) ◽  
pp. 625-640 ◽  
Author(s):  
Deri Morgan ◽  
Boris Musset ◽  
Kethika Kulleperuma ◽  
Susan M.E. Smith ◽  
Sindhu Rajan ◽  
...  
Keyword(s):  
Transmembrane Helix ◽  
Homology Model ◽  
Selectivity Filter ◽  
Proton Channel ◽  
Suppressor Activity ◽  
Voltage Gated ◽  
Anion Permeation ◽  
Hydrogen Bond Networks ◽  
Conduction Pathway ◽  
Dynamics Simulations

Extraordinary selectivity is crucial to all proton-conducting molecules, including the human voltage-gated proton channel (hHV1), because the proton concentration is >106 times lower than that of other cations. Here we use “selectivity filter scanning” to elucidate the molecular requirements for proton-specific conduction in hHV1. Asp112, in the middle of the S1 transmembrane helix, is an essential part of the selectivity filter in wild-type (WT) channels. After neutralizing Asp112 by mutating it to Ala (D112A), we introduced Asp at each position along S1 from 108 to 118, searching for “second site suppressor” activity. Surprisingly, most mutants lacked even the anion conduction exhibited by D112A. Proton-specific conduction was restored only with Asp or Glu at position 116. The D112V/V116D channel strikingly resembled WT in selectivity, kinetics, and ΔpH-dependent gating. The S4 segment of this mutant has similar accessibility to WT in open channels, because R211H/D112V/V116D was inhibited by internally applied Zn2+. Asp at position 109 allowed anion permeation in combination with D112A but did not rescue function in the nonconducting D112V mutant, indicating that selectivity is established externally to the constriction at F150. The three positions that permitted conduction all line the pore in our homology model, clearly delineating the conduction pathway. Evidently, a carboxyl group must face the pore directly to enable conduction. Molecular dynamics simulations indicate reorganization of hydrogen bond networks in the external vestibule in D112V/V116D. At both positions where it produces proton selectivity, Asp frequently engages in salt linkage with one or more Arg residues from S4. Surprisingly, mean hydration profiles were similar in proton-selective, anion-permeable, and nonconducting constructs. That the selectivity filter functions in a new location helps to define local environmental features required to produce proton-selective conduction.

scholarly journals Influence of Proline Residues in Transmembrane Helix Packing

2004 ◽  
Vol 335 (2) ◽  
pp. 631-640 ◽  
Author(s):  
Mar Orzáez ◽  
Jesús Salgado ◽  
Ana Giménez-Giner ◽  
Enrique Pérez-Payá ◽  
Ismael Mingarro
Keyword(s):  
Transmembrane Helix ◽  
Helix Packing
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