Publication Abstract from PubMed
The crystal structure of an N-terminal beta-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 beta-strand swapping, leading to the formation of a stable compact dimer. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
N-terminal beta-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.,Luo J, Teplyakov A, Obmolova G, Malia TJ, Chan W, Jacobs SA, O'Neil KT, Gilliland GL Proteins. 2014 Jan 27. doi: 10.1002/prot.24517. PMID:24464739[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
