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N‐terminal β‐strand swapping in a consensus‐derived alternative scaffold driven by stabilizing hydrophobic interactions
Author(s) -
Luo Jinquan,
Teplyakov Alexey,
Obmolova Galina,
Malia Thomas J.,
Chan Winnie,
Jacobs Steven A.,
O'Neil Karyn T.,
Gilliland Gary L.
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24517
Subject(s) - dimer , hydrophobic effect , chemistry , biophysics , crystallography , terminal (telecommunication) , stereochemistry , scaffold , biochemistry , organic chemistry , computer science , biology , database , telecommunications
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.