Effect of transmembrane helix packing on tryptophan and tyrosine environments in detergent-solubilized bacterio-opsin

1996 ◽  
Vol 15 (3) ◽  
pp. 281-289 ◽  
Author(s):  
Robert Renthal ◽  
Patrick Haas
Keyword(s):  
Transmembrane Helix ◽  
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 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 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

Coaction of Electrostatic and Hydrophobic Interactions: Dynamic Constraints on Disordered TrkA Juxtamembrane Domain

2019 ◽  
Author(s):  
Zichen Wang ◽  
Huaxun Fan ◽  
Xiao Hu ◽  
John Khamo ◽  
Jiajie Diao ◽  
...  
Keyword(s):  
Single Molecule ◽  
Protein Function ◽  
Hydrophobic Interactions ◽  
Transmembrane Helix ◽  
Point Mutations ◽  
Salt Bridge ◽  
Receptor Activation ◽  
Membrane Dynamics ◽  
Juxtamembrane Domain ◽  
Joint Work

<p>The receptor tyrosine kinase family transmits signals into cell via a single transmembrane helix and a flexible juxtamembrane domain (JMD). Membrane dynamics makes it challenging to study the structural mechanism of receptor activation experimentally. In this study, we employ all-atom molecular dynamics with Highly Mobile Membrane-Mimetic to capture membrane interactions with the JMD of tropomyosin receptor kinase A (TrkA). We find that PIP<sub>2 </sub>lipids engage in lasting binding to multiple basic residues and compete with salt bridge within the peptide. We discover three residues insertion into the membrane, and perturb it through computationally designed point mutations. Single-molecule experiments indicate the contribution from hydrophobic insertion is comparable to electrostatic binding, and in-cell experiments show that enhanced TrkA-JMD insertion promotes receptor ubiquitination. Our joint work points to a scenario where basic and hydrophobic residues on disordered domains interact with lipid headgroups and tails, respectively, to restrain flexibility and potentially modulate protein function.</p>

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