Ulteriori informazioni
Since the full functionality of any given protein can only be understood in terms of its interaction with other, often regulatory proteins, this unique reference source covers all relevant protein domains, including SH2, SH3, PDZ, WW, PTB, EH, PH and PX. Its user-oriented concept combines broad coverage with easy retrieval of essential information, and includes a special section on Web-based tools and databases covering protein modules and functional peptide motifs.Essential for the study of protein-protein interactions in vivo or in silico, and a prerequisite for successful functional proteomics studies.With a prologue by Sir Tom Blundell.
Sommario
INTRODUCTIONAn overview of protein to protein interactions and protein modulesSH2 domain as a paradigm of protein modulesPROTEIN BINDING DOMAINS THAT INTERACT WITH PROLINE LIGANDSSH3 domainWW domainEVH1 domainGYF domainPROTEIN BINDING DOMAINS AND THEIR REGULATION BY PHOSPHORYLATIONPTB domainFHA domains14-3-3 proteins and phospho-serine/theronine binding modulesProtein kinase domains as important catalytic domains functionally linked to protein binding domainsPROTEIN DOMAINS REGULATING CHROMATIN FUNCTIONSET domainsBromo domainChromo & Shadow-Chromo domainsPROTEIN DOMAINS RECOGNIZING SHORT PEPTIDE CORES IN THEIR LIGANDSPDZ domainEH domainEXAMPLES OF FUNCTIONAL DIVERSITY AMONG PROTEIN DOMAINS: UBIQUITIN AND ACTIN BINDING DOMAINSUbiquitin-Binding DomainsCH domainPHOSPHO-INOSITIDE BINDING PROTEIN DOMAINSPH domainVHS and ENTH domainsPX domainDISSECTING DOMAINS AND LIGANDS WITH PEPTIDE CHEMISTRY AND COMPUTERSPeptide and protein repertoires for global analysis of modulesComputational analysis of modular protein domainsNomenclatures for protein modules and their cognate motifsEPILOGUE: Future perspectives
Info autore
Gianni Cesareni is a Full Professor of Genetics at the University of Rome Tor Vergata (Italy). After obtaining a degree in physics at the University of Rome La Sapienza he spent three years in Cambridge in the laboratory of Sidney Brenner. He then moved to the EMBL in Heidelberg where he led a group working on the mechanisms controlling plasmid DNA replication. Since 1989 he teaches and works in Rome. He is interested in the interplay between specificity and promiscuity in the protein interaction network mediated by protein recognition modules.
Mario Gimona is laboratory head at the Consorzio Mario Negri Sud in Santa Maria Imbaro (Italy) and reader for molecular cell biology at the University of Salzburg (Austria). He was born in Salzburg where he also received his degrees in genetics and biochemistry, after completing his Ph.D. work in the lab of Vic Small at the Austrian Academy of Sciences. Following his post-doctoral time at the CSHL, New York (USA) with David Helfman he set up his own laboratory in Salzburg at the OeAW in 1996. His research interests revolve around the linguistic variation of functional protein modules and their role in the regulation of the actin cytoskeleton.
Marius Sudol has been an Associate Professor at the Mount Sinai School of Medicine in New York since 1995. He was instrumental in the delineation and characterization of one of the smallest protein modules, the WW domain. His work also implicated the WW domain in signaling pathways underlying several human diseases including Alzheimer's disease, hypertension and cancer. He earned a Ph.D. at The Rockefeller University in New York in 1983 and stayed at his Alma Mater as a postdoctoral fellow and faculty member until his move to Mount Sinai. Dr.Sudol has published 95 research articles and is credited as inventor on two biotechnology patents.
Michael B. Yaffe is Associate Professor of Biology at the Center for Cancer Research, Massachusetts Institute of Technology. He earned his MD and PhD degrees at Case Western Reserve University, and did residency training in general surgery, trauma and critical care medicine at Harvard Medical School. He was a post-doctoral fellow in Cell Biology at Harvard under Lewis C. Cantley, where he remained as junior faculty until moving to MIT in 2000. He is interested in signal transduction, protein phosphorylation, and phosphopeptide-binding domains, with a focus on cell cycle control, DNA damage responses, and inflammation.
All editors are members of the "Protein Module Consortium", a world-wide organization to support researchers interested in protein modules.
Riassunto
Um die Funktionalität eines Proteins vollständig zu erfassen, muss man seine Wechselwirkungen mit anderen Proteinen verstehen. Alle dafür relevanten Proteindomänen (SH2, SH3, PDZ, WW, PTB, EH, PH und PX) erfasst dieses in seiner Art einmalige Nachschlagewerk. Der Stoff wurde sinnvoll ausgewählt, geordnet und mit Verweisen versehen, sodass man gewünschte Informationen schnell findet. Ein spezielles Kapitel stellt Hilfsmittel und relevante Datenbanken vor, die kostenlos aus dem Internet heruntergeladen werden können. Unentbehrlich für alle, die Wechselwirkungen zwischen Proteinen in vivo oder in silico (am Computer) untersuchen oder sich mit Proteomik beschäftigen.
Relazione
"... the book is well written and provides clear, concise and informative reviews on some of the most common domains involved in protein-peptide interactions."Nature Cell Biology, July 2005
