Computational model for the IGF‐II/IGF2r complex that is predictive of mutational and surface plasmon resonance data

Computational model for the IGF‐II/IGF2r complex that is predictive of mutational and surface plasmon resonance data

Source :

• Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 2006-08-15.

English descriptors

• KwdEn :
  • Accessible surface area, Acta crystallogr, Aliphatic residues, Aromatic residues, Binding, Binding protein interactions, Binding site, Binding sites, Bioinformatics, Biol, Biol chem, Biological data, Black line, Breast cancer, Cancer research, Chem, Complementarity, Complex formation, Constraint, Crystal structure, Different types, Docking, Docking procedure, Docking process, Docking simulations, Electrostatic interactions, Energy minimization, Exible, Exible loop, Experimental evidence, Filter module, Ftdock, Growth factor, Growth factor binding proteins, Growth factors, Human growth factor, Hydrogen bonds, Hydrophobic, Hydrophobic groove, Igf2r, Igf2r binding, Igf2r fragment, Igf2r fragments, Interaction energy, Interface, Kinetic analysis results, Kinetic data, Langmuir binding model, Ltering process, Mannose receptor, Medical research council, Minimization, Model complexes, Multidock, Mutagenesis, National health, Pair potentials, Perl script, Previous analysis, Principal axes, Proc natl acad, Protein data bank, Protein interfaces, Protein surface, Putative, Putative binding site, Putative complexes, Putative interface, Receptor, Residue, Rmsd, Rpscore, Salt bridges, Shape complementarity, Silico, Silico analysis, Solution structure, Solution structures, Steady state model, Structural biology, Supplementary material, Surface area, Surface characteristics, Surface plasmon resonance, Surface plasmon resonance analysis, Unbound.
• Teeft :
  • Accessible surface area, Acta crystallogr, Aliphatic residues, Aromatic residues, Binding, Binding protein interactions, Binding site, Binding sites, Bioinformatics, Biol, Biol chem, Biological data, Black line, Breast cancer, Cancer research, Chem, Complementarity, Complex formation, Constraint, Crystal structure, Different types, Docking, Docking procedure, Docking process, Docking simulations, Electrostatic interactions, Energy minimization, Exible, Exible loop, Experimental evidence, Filter module, Ftdock, Growth factor, Growth factor binding proteins, Growth factors, Human growth factor, Hydrogen bonds, Hydrophobic, Hydrophobic groove, Igf2r, Igf2r binding, Igf2r fragment, Igf2r fragments, Interaction energy, Interface, Kinetic analysis results, Kinetic data, Langmuir binding model, Ltering process, Mannose receptor, Medical research council, Minimization, Model complexes, Multidock, Mutagenesis, National health, Pair potentials, Perl script, Previous analysis, Principal axes, Proc natl acad, Protein data bank, Protein interfaces, Protein surface, Putative, Putative binding site, Putative complexes, Putative interface, Receptor, Residue, Rmsd, Rpscore, Salt bridges, Shape complementarity, Silico, Silico analysis, Solution structure, Solution structures, Steady state model, Structural biology, Supplementary material, Surface area, Surface characteristics, Surface plasmon resonance, Surface plasmon resonance analysis, Unbound.

Abstract

• https://api.istex.fr/document/27EF09D8D60BFED4B3EF506117CC740F39008D2D/fulltext/pdf

Affiliations:

• Australie, France, Royaume-Uni, États-Unis
• Angleterre, Californie, Oxfordshire, Provence-Alpes-Côte d'Azur
• Marseille, Oxford
• Université d'Oxford

Links toward previous steps (curation, corpus...)

• to stream Istex, to step Corpus: 000775
• to stream Istex, to step Curation: 000775
• to stream Istex, to step Checkpoint: 001678
• to stream Main, to step Merge: 00A489
• to stream Main, to step Curation: 009A25

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