The GxxxG motif: a framework for transmembrane helix-helix association.

By W. P. Russ, Donald M. Engelman. Journal of Molecular Biology, 2000

969 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a779d17e1b21b4f85099212981d8ad950e659f66

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In Molecular Biology

1. Mark Gerstein
2. Alessandro Senes
3. Christoph Peters
4. Steven O. Smith
5. Donald M. Engelman

Citations in the corpus

• Comparison of Helix Interactions in Membrane and Soluble α-Bundle Proteins (2002, background): “, 2000) and dimerization-dependent screens (Russ and Engelman, 2000) for helix interactions in membrane proteins having single membrane spanning helices.”
• The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. (2012, neutral): “Generally, the GXXXG motif or glycine zipper motif enables close packing of transmembrane helixes (Brosig and Langosch, 1998; Curran and Engelman, 2003; Kim et al., 2005; Russ and Engelman, 2000).”
• Topology Prediction of α-Helical Transmembrane Proteins (2016, background): “Glycine is not only interesting in combination with proline, but also in form of the GXXXG motifs that play a role in helix-helix packing interactions [41].”
• Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. (2000, methodology): “…with the TOXCAT in vivo selection system for helix-helix interaction The GG4 pair is almost invariably present in the transmembrane oligomerization motifs identi®ed from randomized sequences by the TOXCAT in vivo selection system, presented in the accompanying paper (Russ & Engelman, 2000).”