Cited by 1,988Protein Structure and Dynamicsthermodynamics and calorimetric analysesEnzyme Structure and Function

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Anatomy of hot spots in protein interfaces

Bogan, Andrew A, Thorn, Kurt S·1998·Journal of Molecular Biology

DOI 10.1006/jmbi.1998.1843

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Abstract

Binding of one protein to another is involved in nearly all biological functions, yet the principles governing the interaction of proteins are not fully understood. To analyze the contributions of individual amino acid residues in protein-protein binding we have compiled a database of 2325 alanine mutants for which the change in free energy of binding upon mutation to alanine has been measured (available at http://motorhead. ucsf.edu/thorn/hotspot). Our analysis shows that at the level of side-chains there is little correlation between buried surface area and free energy of binding. We find that the free energy of binding is not evenly distributed across interfaces; instead, there are hot spots of binding energy made up of a small subset of residues in the dimer interface. These hot spots are enriched in tryptophan, tyrosine and arginine, and are surrounded by energetically less important residues that most likely serve to occlude bulk solvent from the hot spot. Occlusion of solvent is found to be a necessary condition for highly energetic interactions.

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Authors: Bogan, A. A., & Thorn, K. S.
Affiliations: University of California, San Francisco (US)
Corresponding author: Bogan, Andrew A
ORCID: Thorn, Kurt S
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 1998-07
Volume: 280
Issue: 1
Pages: 1-9
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1006/jmbi.1998.1843
OpenAlex: W2051710717
Cited by: 1,988
References: 71
Citations by year: 2026: 62 · 2025: 52 · 2024: 68 · 2023: 40 · 2022: 51 · 2021: 75 · 2020: 69 · 2019: 65 · 2018: 77 · 2017: 75 · 2016: 94 · 2015: 105 · 2014: 88 · 2013: 110 · 2012: 112
FWCI: 11.85
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: protein-protein binding, binding hot spots, alanine scanning, binding free energy, protein interfaces, buried surface area, tryptophan, tyrosine, L-arginine, dimer interface, binding energy distribution
MeSH terms: Alanine, Amino Acids, Binding Sites, Humans, Protein Binding, Proteins, Structure-Activity Relationship

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Anatomy of hot spots in protein interfaces

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