4M6A

N-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by Stabilizing Hydrophobic Interactions

Summary for 4M6A

• Entry DOI: 10.2210/pdb4m6a/pdb
• Related: 3tes
• Descriptor: Tencon (2 entities in total)
• Functional Keywords: tencon, fn3-like domain, alternative scaffold, b-strand swapping, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 10
• Total formula weight: 99019.54

Authors

Luo, J.,Teplyakov, A.,Obmolova, G.,Malia, T.J.,Chan, W.,Jocobs, S.A.,O'neil, K.T.,Gilliland, G.L. (deposition date: 2013-08-09, release date: 2014-02-26, Last modification date: 2023-09-20)

Primary citation

Luo, J.,Teplyakov, A.,Obmolova, G.,Malia, T.J.,Chan, W.,Jacobs, S.A.,O'Neil, K.T.,Gilliland, G.L.
N-terminal beta-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.
Proteins, 82:1527-1533, 2014

PubMed 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.

PubMed: 24464739
DOI: 10.1002/prot.24517

Experimental method

X-RAY DIFFRACTION (2.71 Å)