Molecular dynamics studies on mutants of Cu, Zn superoxide dismutase: The functional role of charged residues in the electrostatic loop VII

1994 ◽  
Vol 18 (3) ◽  
pp. 216-230 ◽  
Author(s):  
Lucia Banci ◽  
Paolo Carloni ◽  
Pier Luigi Orioli
Keyword(s):  
Molecular Dynamics ◽  
Superoxide Dismutase ◽  
Functional Role ◽  
Charged Residues ◽  
Electrostatic Loop

Molecular dynamics studies on superoxide dismutase and its mutants: the structural and functional role of Arg 143

1992 ◽  
Vol 114 (18) ◽  
pp. 6994-7001 ◽  
Author(s):  
Lucia Banci ◽  
Paolo Carloni ◽  
Giovanni La Penna ◽  
Pier Luigi Orioli
Keyword(s):  
Molecular Dynamics ◽  
Superoxide Dismutase ◽  
Functional Role

scholarly journals Role of the electrostatic loop charged residues in Cu, Zn superoxide dismutase

1998 ◽  
Vol 7 (11) ◽  
pp. 2354-2358 ◽  
Author(s):  
Fabio Polticelli ◽  
Andrea Battistoni ◽  
Peter O'Neill ◽  
Giuseppe Rotilio ◽  
Alessandro Desideri
Keyword(s):  
Superoxide Dismutase ◽  
Charged Residues ◽  
Electrostatic Loop

scholarly journals Functional Role of Charged Residues in the Transmembrane Segments of the Yeast Plasma Membrane H+-ATPase

2000 ◽  
Vol 275 (21) ◽  
pp. 15709-15716 ◽  
Author(s):  
Valery V. Petrov ◽  
Kristine P. Padmanabha ◽  
Robert K. Nakamoto ◽  
Kenneth E. Allen ◽  
Carolyn W. Slayman
Keyword(s):  
Plasma Membrane ◽  
Functional Role ◽  
Yeast Plasma Membrane ◽  
Transmembrane Segments ◽  
Charged Residues

scholarly journals Mechanism of gating by calcium in connexin hemichannels

2016 ◽  
Vol 113 (49) ◽  
pp. E7986-E7995 ◽  
Author(s):  
William Lopez ◽  
Jayalakshmi Ramachandran ◽  
Abdelaziz Alsamarah ◽  
Yun Luo ◽  
Andrew L. Harris ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Small Molecules ◽  
Binding Sites ◽  
General Mechanism ◽  
Salt Bridges ◽  
Charged Residues ◽  
Dynamics Simulations ◽  
Connexin Hemichannel ◽  
Connexin Hemichannels

Aberrant opening of nonjunctional connexin hemichannels at the plasma membrane is associated with many diseases, including ischemia and muscular dystrophy. Proper control of hemichannel opening is essential to maintain cell viability and is achieved by physiological levels of extracellular Ca2+, which drastically reduce hemichannel activity. Here we examined the role of conserved charged residues that form electrostatic networks near the extracellular entrance of the connexin pore, a region thought to be involved in gating rearrangements of hemichannels. Molecular dynamics simulations indicate discrete sites for Ca2+ interaction and consequent disruption of salt bridges in the open hemichannels. Experimentally, we found that disruption of these salt bridges by mutations facilitates hemichannel closing. Two negatively charged residues in these networks are putative Ca2+ binding sites, forming a Ca2+-gating ring near the extracellular entrance of the pore. Accessibility studies showed that this Ca2+-bound gating ring does not prevent access of ions or small molecules to positions deeper into the pore, indicating that the physical gate is below the Ca2+-gating ring. We conclude that intra- and intersubunit electrostatic networks at the extracellular entrance of the hemichannel pore play critical roles in hemichannel gating reactions and are tightly controlled by extracellular Ca2+. Our findings provide a general mechanism for Ca2+ gating among different connexin hemichannel isoforms.

Functional Role of Arginine-11 in the N-Terminal Helix of Skeletal Troponin C: Combined Mutagenesis and Molecular Dynamics Investigation

Biochemistry ◽  
1995 ◽  
Vol 34 (22) ◽  
pp. 7348-7355 ◽  
Author(s):  
Jagdish Gulati ◽  
Arvind B. Akella ◽  
Hong Su ◽  
Ernest L. Mehler ◽  
Harel Weinstein
Keyword(s):  
Molecular Dynamics ◽  
Functional Role ◽  
Troponin C ◽  
Combined Mutagenesis
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