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PDBsum entry 4m6a

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De novo protein PDB id
4m6a
Contents
Protein chains
87 a.a.
(+ 2 more) 91 a.a.
Waters ×182

References listed in PDB file
Key reference
Title N-Terminal β-Strand swapping in a consensus-Derived alternative scaffold driven by stabilizing hydrophobic interactions.
Authors J.Luo, A.Teplyakov, G.Obmolova, T.J.Malia, W.Chan, S.A.Jacobs, K.T.O'Neil, G.L.Gilliland.
Ref. Proteins, 2014, 82, 1527-1533. [DOI no: 10.1002/prot.24517]
PubMed id 24464739
Abstract
The crystal structure of an N-terminal β-strand-swapped consensus-derived tenascin FN3 alternative scaffold has been determined. A comparison with the unswapped structure reveals that the side chain of residue F88 orients differently and packs more tightly with the hydrophobic core of the domain. Dimer formation also results in the burial of a hydrophobic patch on the surface of the domain. Thus, it appears that tighter packing of F88 in the hydrophobic core and burial of surface hydrophobicity provide the driving forces for the N-terminal β-strand swapping, leading to the formation of a stable compact dimer. Proteins 2014; 82:1527-1533. © 2014 Wiley Periodicals, Inc.
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