The molecular architecture of protein-protein binding sites

Dana Reichmann*, Ofer Rahat, Mati Cohen, Hani Neuvirth, Gideon Schreiber

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

180 Scopus citations


The formation of specific protein interactions plays a crucial role in most, if not all, biological processes, including signal transduction, cell regulation, the immune response and others. Recent advances in our understanding of the molecular architecture of protein-protein binding sites, which facilitates such diversity in binding affinity and specificity, are enabling us to address key questions. What is the amino acid composition of binding sites? What are interface hotspots? How are binding sites organized? What are the differences between tight and weak interacting complexes? How does water contribute to binding? Can the knowledge gained be translated into protein design? And does a universal code for binding exist, or is it the architecture and chemistry of the interface that enable diverse but specific binding solutions?

Original languageAmerican English
Pages (from-to)67-76
Number of pages10
JournalCurrent Opinion in Structural Biology
Issue number1
StatePublished - Feb 2007
Externally publishedYes

Bibliographical note

Funding Information:
This work was funded by MINERVA (grant 8525) and the Israeli Ministry of Science and Technology (grant 0263).


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