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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding
Author(s) -
Weber Mathias,
Schneider Dirk
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.03.039
Subject(s) - transmembrane domain , dimer , helix (gastropod) , transmembrane protein , sequence (biology) , amino acid , peptide sequence , hydrogen bond , chemistry , context (archaeology) , crystallography , stereochemistry , biochemistry , biology , gene , molecule , ecology , paleontology , receptor , organic chemistry , snail
Distinct 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.