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Domain binding and function:Src-homology 3 (SH3) domains bind to Pro-rich peptides that form a left-handed poly-Pro type II helix, with the minimal consensus Pro-X-X-Pro. Each Pro is usually preceded by an aliphatic residue. Each in the aliphatic-Pro pair binds to a hydrophobic pocket on the SH3 domain. The ligand can, in principle, bind in either orientation. An additional non-Pro residue, frequently Arg, can form part of the binding core and contacts the SH3 domain. Such peptides usually bind to the SH3 domain with a Kd in the µM range. The binding affinity and specificity can be markedly increased by tertiary interactions involving loops on the SH3 domain. Structure Reference: Lim, W.A. et al. (1994) Nature 372(6504), 375¿379. Examples of Domain Proteins:

The C-terminal SH3 domain of SEM-5 bound to mSOS peptide (red).

Binding Examples:

	SH3 domain proteins		Binding partners		SH3 domain binding sites
	Src Tyrosine Kinase		p85 subunit of Pl3 kinase		RPLPVAP Class l N-terminal to C-terminal binding site
	Crk Adaptor Protein		C3G guanidine nucleotide exchanger		PPPALPPKKR Class ll C-terminal to N-terminal binding site