RSS

PDB:1L2Y

Protein Name

Trp-cage designed protein TC5b

Species

N/A (synthetic)

Biological Context

The design and structural characterization of miniproteins with a compact, folded structure provides insights into the protein folding and unfolding pathways including the minimum requirements for a protein sequence to fold.

Structure Description

1l2y1l2y_x1l2y_y

In this article, a 20-residue protein that folds into a novel 'Trp-cage' motif is reported. With a poorly folded 39-residue peptide as a starting point, truncation and mutaion of the peptide has produced a 20-residue construct that is well folded in water at physiological pH. NMR measurements have shown that the Trp-cage with two proline residues on each side of the Trp indole ring plus Tyr makes up the hydrophobic core and that the Trp side-chain is 100% buried in aqueous solution. The NMR structure of the Trp-cage motif shows important features typical of a small protein. It has multiple secondary structural elements, side chain-side chain packing interactions, well defined tertiary contacts and a compact overall structure. On account of the small size, the architectural simplicity and the limited conformational flexibility, the Trp-cage miniprotein is expected to be useful for both experimental studies and computational simulations of protein folding and unfolding pathways.

Protein Data Bank (PDB)

References

Source

Neidigh, J.W. Fesinmeyer, R.M. Andersen, N.H.; "Designing a 20-residue protein."; Nat.Struct.Biol.; (2002) 9:425-430 PubMed:11979279.

Others

author: Aki Nagata


Japanese version:PDB:1L2Y