Acta Crystallographica Section F Structural Biology Communications · 2015 · 36 citations · 18 references
Life SciencesMedicinal ChemistryMolecular BiologyApoptosisProtein-protein InteractionsStructural BiologyApoptotic SignalingDeath ReceptorsLigand BindingReceptor-ligand InteractionsApoptosis-inducing FactorCell Surface Death ReceptorsLigand-receptor Binding SpecificityProtein-protein Interactions In ApoptosisReceptor-ligand Structural BiologySequence SimilarityTrail ReceptorsTumor Necrosis Factor-related Apoptosis-inducing Ligand Receptors
The structure of death receptor 4 (DR4) in complex with TNF-related apoptosis-inducing ligand (TRAIL) has been determined at 3 Å resolution and compared with those of previously determined DR5-TRAIL complexes. Consistent with the high sequence similarity between DR4 and DR5, the overall arrangement of the DR4-TRAIL complex does not differ substantially from that of the DR5-TRAIL complex. However, subtle differences are apparent. In addition, solution interaction studies were carried out that show differences in the thermodynamics of binding DR4 or DR5 with TRAIL.
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Features and development of <i>Coot</i>
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<i>Phaser</i>crystallographic software
Airlie J. McCoy, Ralf W. Grosse‐Kunstleve, Paul D. Adams et al. · Journal of Applied Crystallography · 2007 · 20.9K citations · Full text
Analytical molecular surface calculation
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