2df5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Certain sequences, known as chameleon sequences, take both alpha- and | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Conformational contagion in a protein: | + | 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 Aug 15;68(3):617-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17510955 17510955] |
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Pyroglutamyl-peptidase I]] | [[Category: Pyroglutamyl-peptidase I]] | ||
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[[Category: pyrrolidone carboxyl peptidase]] | [[Category: pyrrolidone carboxyl peptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:11 2008'' |
Revision as of 14:58, 21 February 2008
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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.
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 Aug 15;68(3):617-25. PMID:17510955
Page seeded by OCA on Thu Feb 21 16:58:11 2008
