Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5HRY

Computationally Designed Cyclic Dimer ank3C2_1

Summary for 5HRY
Entry DOI10.2210/pdb5hry/pdb
Descriptorank3C2_1 (2 entities in total)
Functional Keywordsprotein design, designed oligomeric interface, de novo protein
Biological sourcesynthetic construct
Total number of polymer chains8
Total formula weight144103.08
Authors
Cascio, D.,McNamara, D.E.,Fallas, J.A.,Baker, D.,Yeates, T.O. (deposition date: 2016-01-24, release date: 2017-04-12, Last modification date: 2023-09-27)
Primary citationFallas, J.A.,Ueda, G.,Sheffler, W.,Nguyen, V.,McNamara, D.E.,Sankaran, B.,Pereira, J.H.,Parmeggiani, F.,Brunette, T.J.,Cascio, D.,Yeates, T.R.,Zwart, P.,Baker, D.
Computational design of self-assembling cyclic protein homo-oligomers.
Nat Chem, 9:353-360, 2017
Cited by
PubMed Abstract: Self-assembling cyclic protein homo-oligomers play important roles in biology, and the ability to generate custom homo-oligomeric structures could enable new approaches to probe biological function. Here we report a general approach to design cyclic homo-oligomers that employs a new residue-pair-transform method to assess the designability of a protein-protein interface. This method is sufficiently rapid to enable the systematic enumeration of cyclically docked arrangements of a monomer followed by sequence design of the newly formed interfaces. We use this method to design interfaces onto idealized repeat proteins that direct their assembly into complexes that possess cyclic symmetry. Of 96 designs that were characterized experimentally, 21 were found to form stable monodisperse homo-oligomers in solution, and 15 (four homodimers, six homotrimers, six homotetramers and one homopentamer) had solution small-angle X-ray scattering data consistent with the design models. X-ray crystal structures were obtained for five of the designs and each is very close to their corresponding computational model.
PubMed: 28338692
DOI: 10.1038/nchem.2673
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227111

건을2024-11-06부터공개중

PDB statisticsPDBj update infoContact PDBjnumon