Structural highlights
Publication Abstract from PubMed
Lactococcal oligopeptide-binding protein A (OppA) binds peptides with widely varying length and sequence. We previously hypothesized that a hydrophobic pocket in OppA preferentially binds a hydrophobic peptide side-chain and thus determines its binding register. Two crystal structures of OppA with different nonapeptides now indeed show binding in different registers.
The importance of a hydrophobic pocket for peptide binding in lactococcal OppA.,Berntsson RP, Thunnissen AM, Poolman B, Slotboom DJ J Bacteriol. 2011 Jun 10. PMID:21665971[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berntsson RP, Thunnissen AM, Poolman B, Slotboom DJ. The importance of a hydrophobic pocket for peptide binding in lactococcal OppA. J Bacteriol. 2011 Jun 10. PMID:21665971 doi:10.1128/JB.00447-11
