6533b856fe1ef96bd12b1de3
RESEARCH PRODUCT
Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding
Mathias WeberDirk Schneidersubject
Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein Bindingdescription
AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close packing and inter-helical hydrogen bonding.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2013-04-11 | FEBS Letters |