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TitleSupramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane.
Journal, issue, pagesJ Struct Biol, Vol. 194, Issue 3, Page 375-382, Year 2016
Publish dateMar 22, 2016
AuthorsBertram Daum / Andrea Auerswald / Tobias Gruber / Gerd Hause / Jochen Balbach / Werner Kühlbrandt / Annette Meister /
PubMed AbstractThe 30kDa N-BAR domain of the human Bin1 protein is essential for the generation of skeletal muscle T-tubules. By electron cryo-microscopy and electron cryo-tomography with a direct electron ...The 30kDa N-BAR domain of the human Bin1 protein is essential for the generation of skeletal muscle T-tubules. By electron cryo-microscopy and electron cryo-tomography with a direct electron detector, we found that Bin1-N-BAR domains assemble into scaffolds of low long-range order that form flexible membrane tubules. The diameter of the tubules closely matches the curved shape of the N-BAR domain, which depends on the composition of the target membrane. These insights are fundamental to our understanding of T-tubule formation and function in human skeletal muscle.
External linksJ Struct Biol / PubMed:27016283
MethodsEM (subtomogram averaging)
Resolution36.0 - 50.0 Å
Structure data

EMDB-8126:
Dimeric N-BAR domain of human Bin1 (Amphiphysin2) associated with tubular sarcolemma model membrane
Method: EM (subtomogram averaging) / Resolution: 50.0 Å

EMDB-8127:
Dimeric N-BAR domain of human Bin1 (Amphiphysin2) associated with tubular sarcolemma model membrane
Method: EM (subtomogram averaging) / Resolution: 36.0 Å

Source
  • Homo sapiens (human)

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