Details

Autor(en) / Beteiligte

• Pang, Chi Nam Ignatius
• Hayen, Andrew
• Wilkins, Marc Ronald

Titel

Surface Accessibility of Protein Post-Translational Modifications

Ist Teil von

• Journal of proteome research, 2007-05, Vol.6 (5), p.1833-1845

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2007

Quelle

MEDLINE

Beschreibungen/Notizen

• Protein post-translational modifications are crucial to the function of many proteins. In this study, we have investigated the structural environment of 8378 incidences of 44 types of post-translational modifications with 19 different approaches. We show that modified amino acids likely to be involved in protein−protein interactions, such as ester-linked phosphorylation, methylarginine, acetyllysine, sulfotyrosine, hydroxyproline, and hydroxylysine, are clearly surface associated. Other modifications, including O-GlcNAc, phosphohistidine, 4-aspartylphosphate, methyllysine, and ADP-ribosylarginine, are either not surface associated or are in a protein's core. Artifactual modifications were found to be randomly distributed throughout the protein. We discuss how the surface accessibility of post-translational modifications can be important for protein−protein interactivity. Keywords: post-translational modifications • protein−protein interaction • surface accessibility • intrinsic disorder • domains and linkers