Linked Life Data

17239579

Source:http://linkedlifedata.com/resource/pubmed/id/17239579

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-2-19
pubmed:abstractText
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?
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-76
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The molecular architecture of protein-protein binding sites.
pubmed:affiliation
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't