Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.

ABSTRACT: Functionally required conformational plasticity of transmembrane proteins implies that specific structural motifs have been integrated in transmembrane helices. Surveying a database of transmembrane helices and the large family of G-protein coupled receptors we identified a series of overrepresented motifs associating Pro with either Ser or Thr. Thus, we have studied the conformation of Pro-kinked transmembrane helices containing Ser or Thr residues, in both g+ and g- rotamers, by molecular dynamics simulations in a hydrophobic environment. Analysis of the simulations shows that Ser or Thr can significantly modulate the deformation of the Pro. A series of motifs, such as (S/T)P and (S/T)AP in the g+ rotamer and the TAP and PAA(S/T) motifs in the g- rotamer, induce an increase in bending an

SUBMITTER: Deupi X 

PROVIDER: S-EPMC1303774 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature