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PDBsum entry 4hb5
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De novo protein
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PDB id
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4hb5
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References listed in PDB file
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Key reference
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Title
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Computational design of self-Assembling cyclic protein homo-Oligomers.
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Authors
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J.A.Fallas,
G.Ueda,
W.Sheffler,
V.Nguyen,
D.E.Mcnamara,
B.Sankaran,
J.H.Pereira,
F.Parmeggiani,
T.J.Brunette,
D.Cascio,
T.R.Yeates,
P.Zwart,
D.Baker.
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Ref.
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Nat Chem, 2017,
9,
353-360.
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PubMed id
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Abstract
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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.
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