Thermodynamic studies on the interaction of the third complement component and its inhibitor, compstatin (Q45110737)

9 December 2017

title

Thermodynamic studies on the interaction of the third complement component and its inhibitor, compstatin (English)

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9 December 2017

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9 December 2017

Madan Katragadda

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9 December 2017

language of work or name

English

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publication date

15 October 2004

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Journal of Biological Chemistry

9 December 2017

published in

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9 December 2017

volume

279

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9 December 2017

issue

53

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9 December 2017

page(s)

54987-54995

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Complement therapeutics; history and current progress.

9 December 2017

cites work

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The structural basis of compstatin activity examined by structure-function-based design of peptide analogs and NMR.

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Binding kinetics, structure-activity relationship, and biotransformation of the complement inhibitor compstatin

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Tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry.

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Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione

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Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry

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Bound water molecules and conformational stabilization help mediate an antigen-antibody association

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Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor

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Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase

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The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation

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Thermodynamic characterization of the interaction between TRAF2 and tumor necrosis factor receptor peptides by isothermal titration calorimetry

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Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains.

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Estimation of the hydrophobic effect in an antigen-antibody protein-protein interface

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The hydrophobic effect and the organization of living matter

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Thermodynamics of peptide inhibitor binding to HIV-1 gp41.

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The NMR solution conformation of unligated human cyclophilin A

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Conformational interconversion in compstatin probed with molecular dynamics simulations

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The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study

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Structure of a cytochrome P450-redox partner electron-transfer complex

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Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?

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Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme

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Integrated Computational and Experimental Approach for Lead Optimization and Design of Compstatin Variants with Improved Activity

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21 January 2018

Identifiers

DOI

10.1074/JBC.M409963200

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9 December 2017

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