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calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics
- Source :
- Biochemistry. April 20, 1999, Vol. 38 Issue 16, p5147, 8 p.
- Publication Year :
- 1999
-
Abstract
- A study on Src homology 2 (SH2) domains and their functions investigated the specificity of the phosphopeptide interaction involving the Src SH2 domain and a peptide containing the sequence PQpYEEIPI (pYEEI). The study also probed the energetic coupling between the +1 Glu, +2 Glu and +3 Ile phosphopeptide residues. Among other results, it was found that the Src SH2 domain is quite permissive of conservative substitutions in the EEI motif at all three peptide positions.
Details
- ISSN :
- 00062960
- Volume :
- 38
- Issue :
- 16
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.54713057