Solution NMR of Acetylcholine Binding Protein Reveals Agonist-Mediated Conformational Change of the C-Loop

2006 ◽  
Vol 70 (4) ◽  
pp. 1230-1235 ◽  
Author(s):  
Fan Gao ◽  
Georges Mer ◽  
Marco Tonelli ◽  
Scott B. Hansen ◽  
Thomas P. Burghardt ◽  
...  
Keyword(s):  
Conformational Change ◽  
Binding Protein ◽  
Solution Nmr ◽  
Acetylcholine Binding Protein

In silico Screening and Molecular Interaction Studies of Tetrahydrocannabinol and its Derivatives with Acetylcholine Binding Protein

2018 ◽  
Vol 12 (2) ◽  
pp. 181-190 ◽  
Author(s):  
Priya P. Panigrahi ◽  
Ramit Singla ◽  
Ankush Bansal ◽  
Moacyr Comar Junior ◽  
Vikas Jaitak ◽  
...  
Keyword(s):  
Molecular Interaction ◽  
In Silico ◽  
Binding Protein ◽  
In Silico Screening ◽  
Acetylcholine Binding Protein ◽  
Interaction Studies

scholarly journals Gating Dynamics of the Acetylcholine Receptor Extracellular Domain

2004 ◽  
Vol 123 (4) ◽  
pp. 341-356 ◽  
Author(s):  
Sudha Chakrapani ◽  
Timothy D. Bailey ◽  
Anthony Auerbach
Keyword(s):  
Conformational Change ◽  
Acetylcholine Receptors ◽  
Single Channel ◽  
Extracellular Domain ◽  
Mouse Muscle ◽  
Α Subunit ◽  
Acetylcholine Binding Protein ◽  
Almost All ◽  
Loop 2 ◽  
Sandwich Core

We used single-channel recording and model-based kinetic analyses to quantify the effects of mutations in the extracellular domain (ECD) of the α-subunit of mouse muscle–type acetylcholine receptors (AChRs). The crystal structure of an acetylcholine binding protein (AChBP) suggests that the ECD is comprised of a β-sandwich core that is surrounded by loops. Here we focus on loops 2 and 7, which lie at the interface of the AChR extracellular and transmembrane domains. Side chain substitutions in these loops primarily affect channel gating by either decreasing or increasing the gating equilibrium constant. Many of the mutations to the β-core prevent the expression of functional AChRs, but of the mutants that did express almost all had wild-type behavior. Rate-equilibrium free energy relationship analyses reveal the presence of two contiguous, distinct synchronously-gating domains in the α-subunit ECD that move sequentially during the AChR gating reaction. The transmitter-binding site/loop 5 domain moves first (Φ = 0.93) and is followed by the loop 2/loop 7 domain (Φ = 0.80). These movements precede that of the extracellular linker (Φ = 0.69). We hypothesize that AChR gating occurs as the stepwise movements of such domains that link the low-to-high affinity conformational change in the TBS with the low-to-high conductance conformational change in the pore.

scholarly journals Crystal Structures of a Cysteine-modified Mutant in Loop D of Acetylcholine-binding Protein

2010 ◽  
Vol 286 (6) ◽  
pp. 4420-4428 ◽  
Author(s):  
Marijke Brams ◽  
Elaine A. Gay ◽  
José Colón Sáez ◽  
Albert Guskov ◽  
René van Elk ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Binding Protein ◽  
Acetylcholine Binding Protein

Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein

1993 ◽  
Vol 13 (4) ◽  
pp. 2377-2383
Author(s):  
X Li ◽  
P Coffino
Keyword(s):  
Conformational Change ◽  
Ornithine Decarboxylase ◽  
Binding Protein ◽  
Active Form ◽  
Feedback Regulation ◽  
Degradation Process ◽  
Protein Inhibitor ◽  
Inhibitory Protein ◽  
C Terminus ◽  
N Terminus

Polyamine-mediated degradation of vertebrate ornithine decarboxylase (ODC) is associated with the production of antizyme, a reversible tightly binding protein inhibitor of ODC activity. The interaction of antizyme with a binding element near the N terminus of ODC is essential but not sufficient for regulation of the enzyme by polyamines (X. Li and P. Coffino, Mol. Cell. Biol. 12:3556-2562, 1992). We now show that a second element present at the C terminus is required for the degradation process. Antizyme caused a conformational change in ODC, which made the C terminus of ODC more accessible. Blocking the C terminus with antibody prevented degradation. Tethering the C terminus by creating a circularly permuted, enzymatically active form of ODC prevented antizyme-mediated degradation. These data elucidate a form of feedback regulation whereby excess polyamines induce destruction of ODC, the enzyme that initiates their biosynthesis.

scholarly journals Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli

2014 ◽  
Vol 9 (1) ◽  
pp. 123-127 ◽  
Author(s):  
Nicolas L. Jean ◽  
Catherine M. Bougault ◽  
Alexander J. F. Egan ◽  
Waldemar Vollmer ◽  
Jean-Pierre Simorre
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Nmr Assignment ◽  
Binding Protein ◽  
Solution Nmr ◽  
Penicillin Binding Protein ◽  
Protein Activator

Evidence for Conformational Change of Fatty Acid-Binding Protein Accompanying Binding of Hydrophobic Ligands1

1994 ◽  
Vol 116 (5) ◽  
pp. 1025-1029 ◽  
Author(s):  
Yoko Honma ◽  
Manabu Niimi ◽  
Toshio Uchiumi ◽  
Yoshiaki Takahashi ◽  
Shoji Odani
Keyword(s):  
Fatty Acid ◽  
Conformational Change ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Structural and Ligand Recognition Characteristics of an Acetylcholine-binding Protein fromAplysia californica

2004 ◽  
Vol 279 (23) ◽  
pp. 24197-24202 ◽  
Author(s):  
Scott B. Hansen ◽  
Todd T. Talley ◽  
Zoran Radić ◽  
Palmer Taylor
Keyword(s):  
Binding Protein ◽  
Ligand Recognition ◽  
Acetylcholine Binding Protein
Sign in / Sign up

Export Citation Format

Share Document