A. Musacchio, M. Noble, R. Pauptit, R. Wierenga, M. Saraste, "Crystal structure of a Src-homology 3 (SH3) domain," Nature, 359:851-5, 1992.

Matti Saraste (European Molecular Biology Laboratory, Heidelberg, Germany): "Many proteins that function in the signaling pathways of animal cells or yeast are made up of distinct domains. These are common to a number of proteins and have structural or functional independence. The SH3 domain is one such mobile protein module.

"SH3 was discovered by comparing amino acid sequences among several different signaling and cytoskeletal proteins. It was called `Src-homology 3,' after Src, the prototype protein tyrosine kinase. The SH3 domain is often accompanied by the SH2 domain, which is made up of about 100 amino acids and recognizes a peptide containing a phosphorylated tyrosine in a specific sequence environment. SH2 is a module that is used for specific interactions between phosphorylated receptors and their downstream partners in signal transduction....

Interested in reading more?

Become a Member of

Receive full access to digital editions of The Scientist, as well as TS Digest, feature stories, more than 35 years of archives, and much more!