Complex Patterns of Histidine, Hydroxylated Amino Acids and the GxxxG Motif Mediate High-affinity Transmembrane Domain Interactions

• Published in: Journal of molecular biology Vol. 385; no. 3; pp. 912 - 923
• Main Authors: Herrmann, Jana R., Panitz, Johanna C., Unterreitmeier, Stephanie, Fuchs, Angelika, Frishman, Dmitrij, Langosch, Dieter
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 23.01.2009
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Amino Acids - metabolism; Blotting, Western; Cell Membrane - metabolism; heterotypic; Histidine; Histidine - chemistry; Histidine - metabolism; Hydroxylation; interaction; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; ToxR/POSSYCCAT; transmembrane domain; POSSYCCAT; ToxR; Histidine; transmembrane domain; BNIP3; ToxR/POSSYCCAT; IPTG; interaction; MalE; TMD; heterotypic; β-gal

Specific interactions of transmembrane helices play a pivotal role in the folding and oligomerization of integral membrane proteins. The helix–helix interfaces frequently depend on specific amino acid patterns. In this study, a heptad repeat pattern was randomized with all naturally occurring amino...