The molecular architecture of protein-protein binding sites

Dana Reichmann; Ofer Rahat; Mati Cohen; Hani Neuvirth; Gideon Schreiber

doi:10.1016/j.sbi.2007.01.004

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 journal › Review article › peer-review

184 Scopus citations

Abstract

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 language	English
Pages (from-to)	67-76
Number of pages	10
Journal	Current Opinion in Structural Biology
Volume	17
Issue number	1
DOIs	https://doi.org/10.1016/j.sbi.2007.01.004
State	Published - Feb 2007
Externally published	Yes

Bibliographical note

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

Access to Document

10.1016/j.sbi.2007.01.004

Cite this

@article{9ab768c6e0a9441fbdca29382d8dc841,

title = "The molecular architecture of protein-protein binding sites",

abstract = "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?",

author = "Dana Reichmann and Ofer Rahat and Mati Cohen and Hani Neuvirth and Gideon Schreiber",

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

year = "2007",

month = feb,

doi = "10.1016/j.sbi.2007.01.004",

language = "אנגלית",

volume = "17",

pages = "67--76",

journal = "Current Opinion in Structural Biology",

issn = "0959-440X",

publisher = "Elsevier Ltd.",

number = "1",

}

TY - JOUR

T1 - The molecular architecture of protein-protein binding sites

AU - Reichmann, Dana

AU - Rahat, Ofer

AU - Cohen, Mati

AU - Neuvirth, Hani

AU - Schreiber, Gideon

N1 - Funding Information: This work was funded by MINERVA (grant 8525) and the Israeli Ministry of Science and Technology (grant 0263).

PY - 2007/2

Y1 - 2007/2

N2 - 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?

AB - 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?

UR - http://www.scopus.com/inward/record.url?scp=33846925964&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2007.01.004

DO - 10.1016/j.sbi.2007.01.004

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.systematicreview???

C2 - 17239579

AN - SCOPUS:33846925964

SN - 0959-440X

VL - 17

SP - 67

EP - 76

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 1

ER -

The molecular architecture of protein-protein binding sites

Abstract

Bibliographical note

Access to Document

Other files and links

Fingerprint

Cite this