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Báo cáo y học: "Sequence patches on MAPK surfaces define protein-protein interactions"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Sequence patches on MAPK surfaces define protein-protein interactions | Minireview Sequence patches on MAPK surfaces define protein-protein interactions Gary L Johnson and Shawn M Gomez Addresses Department of Pharmacology and Lineberger Comprehensive Cancer Center University of North Carolina School of Medicine Chapel Hill NC 27599-7365 USA. Joint Department of Biomedical Engineering University of North Carolina School of Medicine Chapel Hill NC 27599-7365 USA. Correspondence Gary L Johnson. E-mail glj@med.unc.edu Published 5 June 2009 Genome Biology 2009 10 222 doi l0.ll86 gb-2009-l0-6-222 The electronic version of this article is the complete one and can be found online at http genomebiology.com 2009 l0 6 222 2009 BioMed Central Ltd Abstract Recent studies on the modularity of mitogen-activated protein kinases show how redesigning surface patches on a protein can change the topology of a signaling network. In cells protein-protein interaction domains control the organization of multiprotein complexes in signal transduction networks thereby determining the responses of cells to many different stimuli 1 . Such domains are generally defined as independently folded structural modules that can bind a protein ligand or a peptide motif. There are at least 81 defined protein-interaction domains in eukaryotic cells that control the organization and responses of signaling networks 2 . Even a given domain can have significant complexity and be used repeatedly in different contexts. For example more than 120 Src-homology 2 SH2 domains - which recognize phospho-tyrosines - are encoded in the human genome. Each SH2 domain has amino acid variations that alter the sequence context within which it recognizes a phospho-tyrosine residue. In higher eukaryotes especially a single protein is typically composed of multiple domains and so the ability to reconfigure the repertoire of domain composition and position within a protein provides a powerful mechanism for reconfiguring the architecture of signaling networks both in evolution and by design .