Electrostatic complementarity at protein/protein interfaces 1 1Edited by B. Honig

McCoy, Airlie J.; Epa, V. Chandana; Colman, Peter M.

doi:10.1006/jmbi.1997.0987

Cited by 243 publications

(232 citation statements)

References 52 publications

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“…We have adapted the approach of McCoy et al (1997) to explore whether the extended set of complex structures available to date confirms the previous observation that authentic protein-protein interfaces are characterized by experiencing a potential field generated by one binding partner that is complementary in character to the potential field generated by the other.…”

Section: Electrostaticssupporting

confidence: 52%

Computational analyses of the surface properties of protein–protein interfaces

Gruber

Zawaira

Saunders

et al. 2006

Acta Crystallogr D Biol Crystallogr

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Several potential applications of structural biology depend on discovering how one macromolecule might recognize a partner. Experiment remains the best way to answer this question, but computational tools can contribute where this fails. In such cases, structures may be studied to identify patches of exposed residues that have properties common to interaction surfaces and the locations of these patches can serve as the basis for further modelling or for further experimentation. To date, interaction surfaces have been proposed on the basis of unusual physical properties, unusual propensities for particular amino-acid types or an unusually high level of sequence conservation. Using the CXXSurface toolkit, developed as a part of the CCP4MG program, a suite of tools to analyse the properties of surfaces and their interfaces in complexes has been prepared and applied. These tools have enabled the rapid analysis of known complexes to evaluate the distribution of (i) hydrophobicity, (ii) electrostatic complementarity and (iii) sequence conservation in authentic complexes, so as to assess the extent to which these properties may be useful indicators of probable biological function.

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Section: Electrostaticssupporting

confidence: 52%

Computational analyses of the surface properties of protein–protein interfaces

Gruber

Zawaira

Saunders

et al. 2006

Acta Crystallogr D Biol Crystallogr

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show abstract

“…Hydrophobic interactions are fundamental for protein-protein interactions (74). Interfaces also have about one hydrogen bond per 100 Å 2 of buried surface area and electrostatic complementary (75). Analysis of pairing preferences at protein-protein interfaces corroborate that pairing preferentially occur between residues with complementary properties (76).…”

Section: Lif Binding Site Of Lifr-mentioning

confidence: 83%

Leukemia Inhibitory Factor (LIF), Cardiotrophin-1, and Oncostatin M Share Structural Binding Determinants in the Immunoglobulin-like Domain of LIF Receptor

Plun‐Favreau¹,

Perret²,

Diveu³

et al. 2003

Journal of Biological Chemistry

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“…As a rule, the desolvation cost of the charged groups is lower, since they have favorable interactions with other charges and hydrophilic residues surrounding them [24]. The modern viewpoint suggests the electrostatic complementarity of interacting protein surfaces, instead of charge complementarity [26]. It was proposed that the electrostatic force could promote formation of encounter complexes [27,28] and defines the lifetime of complexes [4].…”

Section: Protein-protein Contacts: Structure Composition and Forcesmentioning

confidence: 99%

Protein‐protein interactions as a target for drugs in proteomics

et al. 2003

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Protein-protein interactions play a central role in numerous processes in the cell and are one of the main fields of functional proteomics. This review highlights the methods of bioinformatics and functional proteomics of protein-protein interaction investigation. The structures and properties of contact surfaces, forces involved in protein-protein interactions, kinetic and thermodynamic parameters of these reactions were considered. The properties of protein contact surfaces depend on their functions. The contact surfaces of permanent complexes resemble domain contacts or the protein core and it is reasonable to consider such complex formation as a continuation of protein folding. Characteristics of contact surfaces of temporary protein complexes share some similarities with active sites of enzymes. The contact surfaces of the temporary protein complexes have unique structure and properties and they are more conservative in comparison with active site of enzymes. So they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations were undertaken to find or design small molecules that block protein dimerization or protein(peptide)-receptor interaction, or, on the contrary, to induce protein dimerization.

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Electrostatic complementarity at protein/protein interfaces 1 1Edited by B. Honig

Cited by 243 publications

References 52 publications

Computational analyses of the surface properties of protein–protein interfaces

Computational analyses of the surface properties of protein–protein interfaces

Leukemia Inhibitory Factor (LIF), Cardiotrophin-1, and Oncostatin M Share Structural Binding Determinants in the Immunoglobulin-like Domain of LIF Receptor

Protein‐protein interactions as a target for drugs in proteomics

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