Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 Science
Cell types often exhibit asymmetric distributions of proteins, lipids, and organelles that are linked to specialized functions, and loss of polarization precedes pathological conditions such as cancer. The cell polarity proteins Par3 and Par6 and the ...
Structural Basis for G Protein-Coupled Receptor Activation
Structural Basis for G Protein-Coupled Receptor Activation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00747/20171010/images/medium/bi-2017-00747c_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00747
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10-10-2017 09:37 PM
[NMR paper] The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Here we introduce a thermodynamic framework, based on analysis of ITC and CD spectroscopy data, that provides experimental description of IDP association in terms of folding and binding contributions which can be predicted using sequence folding propensities and molecular modeling. We show how IDP can...
[NMR paper] Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Related Articles Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Biochemistry. 2013 May 31;
Authors: Ali R, Kumar S, Balaram H, Sarma SP
Abstract
The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the...
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06-04-2013 06:31 PM
[NMR paper] Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Related Articles Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Biochim Biophys Acta. 2013 Apr 19;
Authors: Farina B, Doti N, Pirone L, Malgieri G, Pedone EM, Ruvo M, Fattorusso R
Abstract
PED/PEA15 is a small protein involved in many protein-protein interactions that modulates the function of a number of key cellular effectors involved in...
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04-24-2013 09:48 PM
Solid-state NMR and SAXS studies provide a structural basis for the activation of alp
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Related Articles Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Nat Struct Mol Biol. 2010 Aug 29;
Authors: Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H
The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on...
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08-31-2010 09:42 PM
[NMR paper] Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue p
Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Related Articles Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Proteins. 1995 Oct;23(2):196-203
Authors: Graf von Stosch A, Jiménez MA, Kinzel V, Reed J
A close association between the HIV surface protein gp120 and the CD4 T cell receptor initiates the viral multiplication cycle. A 15 amino acid peptide (LAV) within the CD4 binding domain of gp 120 has been shown to retain receptor binding ability. The...
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
Linear Mode
