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Recognition of privileged structures by G-protein coupled receptors.
Privileged structures are ligand substructures that are widely used to generate high-affinity ligands for more than one type of receptor. To explain this, we surmised that there must be some commonExpand
  • 153
  • 7
Location and nature of the residues important for ligand recognition in G‐protein coupled receptors
  • R. Bywater
  • Chemistry, Medicine
  • Journal of molecular recognition : JMR
  • 2005
The overall structure of the biogenic amine subclass of the G‐protein‐coupled receptors, and of their ligand binding sites, is discussed with the aim of highlighting the major structural features ofExpand
  • 51
  • 5
Structure of the integral membrane domain of the GLP1 receptor
A three‐dimensional (3D) model of the integral membrane domain of the GLP1 receptor, a member of the secretin receptor family of the G‐protein‐coupled receptor superfamily is proposed. The probableExpand
  • 60
  • 5
Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.
The conformation of the 20-residue antibiotic ionophore alamethicin in macroscopically oriented phospholipid bilayers has been studied using (15)N solid-state nuclear magnetic resonance (NMR)Expand
  • 96
  • 4
Current progress in Structure-Based Rational Drug Design marks a new mindset in drug discovery
TLDR
The past decade has witnessed a paradigm shift in preclinical drug discovery with structure-based drug design (SBDD) making a comeback while high-throughput screening (HTS) methods have continued to generate disappointing results. Expand
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  • PDF
Prediction of protein residue contacts with a PDB-derived likelihood matrix.
Proteins with similar folds often display common patterns of residue variability. A widely discussed question is how these patterns can be identified and deconvoluted to predict protein structure. InExpand
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  • 4
A sequence and structural study of transmembrane helices
TLDR
A comparison is made between the distribution of residue preferences, three dimensional nearest neighbour contacts, preferred rotamers, helix-helix crossover angles and peptide bond angles in three sets of proteins: a non-redundant set of accurately determined globular protein structures, a set of four helix bundle structures and a set a membrane protein structures. Expand
  • 38
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Toward the active conformations of rhodopsin and the β2‐adrenergic receptor
Using sets of experimental distance restraints, which characterize active or inactive receptor conformations, and the X‐ray crystal structure of the inactive form of bovine rhodopsin as a startingExpand
  • 76
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Domain swapping in G-protein coupled receptor dimers.
Computer simulations were performed on models of the beta2-adrenergic receptor dimer, including 5,6-domain swapped dimers which have been proposed as the active, high affinity form (here the dimerExpand
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  • PDF
Influence of a lipid interface on protein dynamics in a fungal lipase.
Lipases catalyze lipolytic reactions and for optimal activity they require a lipid interface. To study the effect of a lipid aggregate on the behavior of the enzyme at the interfacial plane and howExpand
  • 40
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