Molecular recognition by SH2 domains

摘要: In this chapter, we have described the biophysical investigations which dissected mechanisms of SH2 domain function. Due to nearly a decade and half investigation on domains, much about their binding mechanism has been characterized. domains found positively charged cavity, largely conserved between different coordinates pTyr in target. The ionic interactions pocket pTyr, particular, Arg beta B5 phosphate, provide majority energy stabilizing domain-target interactions. specificity emanates most often from residues C-terminal target determining domain. However, region are weak, hence single show only modest level for tyrosine phosphorylated targets. Greater domain-containing protein-tyrosine can be achieved by placing tandem (as is found) or possibly through specific localization proteins within cell. Although relatively good understanding how function isolation obtained, ways coupled allosteric transmission signals larger still not clear. Hence, future should bring further ligation alters enzymatic activity cellular proteins.