Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Atomic structure of Lanreotide nanotubes revealed by cryo-EM.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 119, Issue 4, Year 2022
Publish date	Jan 25, 2022
Authors	Laura Pieri / Fengbin Wang / Ana-Andreea Arteni / Matthijn Vos / Jean-Marie Winter / Marie-Hélène Le Du / Franck Artzner / Frédéric Gobeaux / Pierre Legrand / Yves Boulard / Stéphane Bressanelli / Edward H Egelman / Maité Paternostre /
PubMed Abstract	Functional and versatile nano- and microassemblies formed by biological molecules are found at all levels of life, from cell organelles to full organisms. Understanding the chemical and ...Functional and versatile nano- and microassemblies formed by biological molecules are found at all levels of life, from cell organelles to full organisms. Understanding the chemical and physicochemical determinants guiding the formation of these assemblies is crucial not only to understand the biological processes they carry out but also to mimic nature. Among the synthetic peptides forming well-defined nanostructures, the octapeptide Lanreotide has been considered one of the best characterized, in terms of both the atomic structure and its self-assembly process. In the present work, we determined the atomic structure of Lanreotide nanotubes at 2.5-Å resolution by cryoelectron microscopy (cryo-EM). Surprisingly, the asymmetric unit in the nanotube contains eight copies of the peptide, forming two tetramers. There are thus eight different environments for the peptide, and eight different conformations in the nanotube. The structure built from the cryo-EM map is strikingly different from the molecular model, largely based on X-ray fiber diffraction, proposed 20 y ago. Comparison of the nanotube with a crystal structure at 0.83-Å resolution of a Lanreotide derivative highlights the polymorphism for this peptide family. This work shows once again that higher-order assemblies formed by even well-characterized small peptides are very difficult to predict.
External links	Proc Natl Acad Sci U S A / PubMed:35042822 / PubMed Central
Methods	EM (helical sym.) / X-ray diffraction
Resolution	0.83 - 2.46 Å
Structure data	13830 7q5a EMDB-13830, PDB-7q5a: Lanreotide nanotube Method: EM (helical sym.) / Resolution: 2.46 Å PDB-7q5g: LAN-DAP5 DERIVATIVE OF LANREOTIDE: L-DIAMINO PROPIONIC ACID IN POSITION 5 IN PLACE OF L-LYSINE Method: X-RAY DIFFRACTION / Resolution: 0.83 Å
Chemicals	ChemComp-EOH: ETHANOL ChemComp-HOH: WATER
Source	homo sapiens (human)
Keywords	HORMONE / Lanreotide / nanotube / assembly