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Irreversible Agonist-Beta2 Adrenoceptor Complex[Membrane Protein/Hydrolase]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT[HYDROLASE]
THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME[HYDROLASE(O-GLYCOSYL)...
DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59[HYDROLASE(O-GLYCOSYL)]
Agonist bound structure of the human adenosine A2a receptor[SIGNALING PROTEIN, HYDROLASE]
Crystal structure of the human beta2 adrenergic receptor in complex with the neutral antagonist alprenolol[MEMBRANE PROTEIN]
Crystal structure of the human beta2 adrenergic receptor in complex with a novel inverse agonist[MEMBRANE PROTEIN]
Crystal structure of the human beta2 adrenergic receptor in complex with the inverse agonist ICI 118,551[MEMBRANE PROTEIN]
The 2.6 A Crystal Structure of a Human A2A Adenosine Receptor bound to ZM241385[MEMBRANE PROTEIN, RECEPTOR]
Cholesterol bound form of human beta2 adrenergic receptor[MEMBRANE PROTEIN]
SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES[HYDROLASE(O-GLYCOSYL)]
N-TERMINAL DOMAIN CORE METHIONINE MUTATION[HYDROLASE]
Structure of a nanobody-stabilized active state of the beta2 adrenoceptor[SIGNALING PROTEIN, Hydrolase]
TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES[HYDROLASE (O-GLYCOSYL)]
CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152C[HYDROLASE]
Structure of the human histamine H1 receptor in complex with doxepin[HYDROLASE]
Structure of the human dopamine D3 receptor in complex with eticlopride[HYDROLASE/HYDROLASE INHIBITOR]
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME[HYDROLASE (O-GLYCOSYL)]
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