Structural Determinants of Transmembrane Helical Proteins

Susan E. Harrington, Nir Ben-Tal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

We identify a structural feature of transmembrane helical proteins that restricts their conformational space and suggests a new way of understanding the construction and stability of their native states. We show that five kinds of well-known specific favorable interhelical interactions (hydrogen bonds, aromatic interactions, salt bridges, and two interactions from packing motifs) precisely determine the packing of the transmembrane helices in 15 diverse proteins. To show this, we iteratively reassemble the helix bundle of each protein using only these interactions, generic interaction geometries, and individual helix backbone conformations. On average, the representative set of rebuilt structures best satisfying the constraints imposed by the five types of interhelical interactions has an average Cα root-mean-square deviation from the native of 1.03 Å. Implications for protein folding, structure and motion prediction, modeling, and design are discussed.

Original languageEnglish
Pages (from-to)1092-1103
Number of pages12
JournalStructure
Volume17
Issue number8
DOIs
StatePublished - 12 Aug 2009

Keywords

  • PROTEINS

Fingerprint

Dive into the research topics of 'Structural Determinants of Transmembrane Helical Proteins'. Together they form a unique fingerprint.

Cite this