3UC7

Trp-cage cyclo-TC1 - monoclinic crystal form

Summary for 3UC7

• Entry DOI: 10.2210/pdb3uc7/pdb
• Related: 2LL5 3UC8
• Descriptor: Cyclo-TC1, CHLORIDE ION (3 entities in total)
• Functional Keywords: mini-protein, trp-cage, cyclic peptide, multimer, protein-protein interaction, de novo protein
• Total number of polymer chains: 6
• Total formula weight: 12936.35

Authors

Scian, M.,Le Trong, I.,Stenkamp, R.E.,Andersen, N.H. (deposition date: 2011-10-26, release date: 2012-07-18, Last modification date: 2024-10-30)

Primary citation

Scian, M.,Lin, J.C.,Le Trong, I.,Makhatadze, G.I.,Stenkamp, R.E.,Andersen, N.H.
Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction.
Proc.Natl.Acad.Sci.USA, 109:12521-12525, 2012

PubMed Abstract: To provide high-resolution X-ray crystallographic structures of a peptide with the Trp-cage fold, we prepared a cyclized version of this motif. Cyclized Trp-cage is remarkably stable and afforded two crystal forms suitable for X-ray diffraction. The resulting higher resolution crystal structures validate the prior NMR models and provide explanations for experimental observations that could not be rationalized by NMR structural data, including the structural basis for the increase in fold stability associated with motif cyclization and the manner in which a polar serine side chain is accommodated in the hydrophobic interior. A hexameric oligomer of the cyclic peptide is found in both crystal forms and indicates that under appropriate conditions, this minimized system may also serve as a model for protein-protein interactions.

PubMed: 22802678
DOI: 10.1073/pnas.1121421109

Experimental method

X-RAY DIFFRACTION (1.1 Å)