Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.

ABSTRACT: Protein-protein interactions occurring via the recognition of short peptide sequences by modular interaction domains play a central role in the assembly of signalling protein complexes and larger protein networks that regulate cellular behaviour. In addition to spatial and temporal factors, the specificity of signal transduction is intimately associated with the specificity of many co-operative, pairwise binding events upon which various pathways are built. Although protein interaction domains are usually identified via the recognition code, the consensus sequence motif, to which they selectively bind, they are highly versatile and play diverse roles in the cell. For example, a given interaction domain can bind to multiple sequences that exhibit no apparent identity, and, on the other hand

SUBMITTER: Li SS 

PROVIDER: S-EPMC1199657 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature