2df5
From Proteopedia
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Crystal Structure of Pf-PCP(1-204)-C
Overview
Certain sequences, known as chameleon sequences, take both alpha- and, beta-conformations in natural proteins. We demonstrate that a wild, chameleon sequence fused to the C-terminal alpha-helix or beta-sheet in, foreign stable proteins from hyperthermophiles forms the same conformation, as the host secondary structure. However, no secondary structural, formation is observed when the sequence is attached to the outside of the, secondary structure. These results indicate that this sequence inherently, possesses an ability to make either alpha- or beta-conformation, depending, on the sequentially neighboring secondary structure if little other, nonlocal interaction occurs. Thus, chameleon sequences take on a satellite, state through contagion by the power of a secondary structure. We propose, this "conformational contagion" as a new nonlocal determinant factor in, protein structure and misfolding related to protein conformational, diseases. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
About this Structure
2DF5 is a Single protein structure of sequence from Pyrococcus furiosus. Active as Pyroglutamyl-peptidase I, with EC number 3.4.19.3 Full crystallographic information is available from OCA.
Reference
Conformational contagion in a protein: Structural properties of a chameleon sequence., Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S, Proteins. 2007 May 17;68(3):617-625. PMID:17510955
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