scholarly journals Conformational analysis of peramivir reveals critical differences between free and enzyme-bound states

MedChemComm ◽  
2014 ◽  
Vol 5 (10) ◽  
pp. 1483-1488 ◽  
Author(s):  
Michele R. Richards ◽  
Michael G. Brant ◽  
Martin J. Boulanger ◽  
Christopher W. Cairo ◽  
Jeremy E. Wulff
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Conformational Change ◽  
Bound States ◽  
Enzyme Binding ◽  
Large Conformational Change ◽  
Conformational Distribution

An analysis of the conformational distribution of peramivir, a potent anti-influenza compound, in solution and the solid state reveals a large conformational change required for enzyme binding.

scholarly journals Reversible Sheet–Turn Conformational Change of a Cell-Penetrating Peptide in Lipid Bilayers Studied by Solid-State NMR

2008 ◽  
Vol 381 (5) ◽  
pp. 1133-1144 ◽  
Author(s):  
Yongchao Su ◽  
Rajeswari Mani ◽  
Tim Doherty ◽  
Alan J. Waring ◽  
Mei Hong
Keyword(s):  
Solid State ◽  
Conformational Change ◽  
Lipid Bilayers ◽  
Solid State Nmr ◽  
Cell Penetrating Peptide ◽  
Cell Penetrating ◽  
A Cell

scholarly journals Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper

2015 ◽  
Vol 6 (12) ◽  
pp. 7311-7318 ◽  
Author(s):  
Claudia Poloni ◽  
Marc C. A. Stuart ◽  
Pieter van der Meulen ◽  
Wiktor Szymanski ◽  
Ben L. Feringa
Keyword(s):  
Secondary Structure ◽  
Conformational Change ◽  
Fiber Formation ◽  
Major Influence ◽  
Heat Control ◽  
Large Conformational Change

The use of an overcrowded alkene photoswitch to control a model β-hairpin peptide is described. The light-induced, large conformational change has major influence on the secondary structure and the aggregation of the peptide, permitting the triggered formation of amyloid-like fibrils.

scholarly journals A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1)

2018 ◽  
Vol 29 (9) ◽  
pp. 1060-1074 ◽  
Author(s):  
Tomohiro Kubo ◽  
Yuqing Hou ◽  
Deborah A. Cochran ◽  
George B. Witman ◽  
Toshiyuki Oda
Keyword(s):  
Conformational Change ◽  
Molecular Mechanism ◽  
Wild Type ◽  
Sliding Direction ◽  
Large Conformational Change ◽  
Dynein Arms ◽  
Biochemical Analyses

Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the f β head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.

Site-Directed Solid-State NMR Measurement of a Ligand-Induced Conformational Change in the Serine Bacterial Chemoreceptor†

Biochemistry ◽  
2001 ◽  
Vol 40 (5) ◽  
pp. 1358-1366 ◽  
Author(s):  
Owen J. Murphy ◽  
Frank A. Kovacs ◽  
Erin L. Sicard ◽  
Lynmarie K. Thompson
Keyword(s):  
Solid State ◽  
Conformational Change ◽  
Solid State Nmr

Sterically Congested Tripodal Phosphites:  Conformational Analysis, Solid-State Polymorphism, Metal Complexation, and Application to the Asymmetric Hydrosilation of Ketones1

2003 ◽  
Vol 42 (17) ◽  
pp. 5097-5106 ◽  
Author(s):  
Sai P. Shum ◽  
Stephen D. Pastor ◽  
Anthony D. DeBellis ◽  
Paul A. Odorisio ◽  
Lilibeth Burke ◽  
...  
Keyword(s):  
Solid State ◽  
Conformational Analysis ◽  
Metal Complexation ◽  
Asymmetric Hydrosilation

scholarly journals Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2

2010 ◽  
Vol 136 (4) ◽  
pp. 407-423 ◽  
Author(s):  
Andras Szollosi ◽  
Paola Vergani ◽  
László Csanády
Keyword(s):  
Conformational Change ◽  
Bound States ◽  
Atp Hydrolysis ◽  
Chloride Ion ◽  
Atp Binding ◽  
Toggle Switch ◽  
Regulatory Domain ◽  
Induced Fit ◽  
Subsequent Formation ◽  
Abc Protein

The chloride ion channel cystic fibrosis transmembrane conductance regulator (CFTR) displays a typical adenosine trisphosphate (ATP)-binding cassette (ABC) protein architecture comprising two transmembrane domains, two intracellular nucleotide-binding domains (NBDs), and a unique intracellular regulatory domain. Once phosphorylated in the regulatory domain, CFTR channels can open and close when supplied with cytosolic ATP. Despite the general agreement that formation of a head-to-tail NBD dimer drives the opening of the chloride ion pore, little is known about how ATP binding to individual NBDs promotes subsequent formation of this stable dimer. Structural studies on isolated NBDs suggest that ATP binding induces an intra-domain conformational change termed “induced fit,” which is required for subsequent dimerization. We investigated the allosteric interaction between three residues within NBD2 of CFTR, F1296, N1303, and R1358, because statistical coupling analysis suggests coevolution of these positions, and because in crystal structures of ABC domains, interactions between these positions appear to be modulated by ATP binding. We expressed wild-type as well as F1296S, N1303Q, and R1358A mutant CFTR in Xenopus oocytes and studied these channels using macroscopic inside-out patch recordings. Thermodynamic mutant cycles were built on several kinetic parameters that characterize individual steps in the gating cycle, such as apparent affinities for ATP, open probabilities in the absence of ATP, open probabilities in saturating ATP in a mutant background (K1250R), which precludes ATP hydrolysis, as well as the rates of nonhydrolytic closure. Our results suggest state-dependent changes in coupling between two of the three positions (1296 and 1303) and are consistent with a model that assumes a toggle switch–like interaction pattern during the intra-NBD2 induced fit in response to ATP binding. Stabilizing interactions of F1296 and N1303 present before ATP binding are replaced by a single F1296-N1303 contact in ATP-bound states, with similar interaction partner toggling occurring during the much rarer ATP-independent spontaneous openings.

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