2dfe

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(New page: 200px<br /><applet load="2dfe" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dfe, resolution 2.40&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17510955 17510955]
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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: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermococcus kodakaraensis]]
[[Category: thermococcus kodakaraensis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:33:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:16 2008''

Revision as of 14:58, 21 February 2008


2dfe, resolution 2.40Å

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Crystal structure of Tk-RNase HII(1-200)-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

2DFE is a Single protein structure of sequence from Thermococcus kodakarensis. Active as Ribonuclease H, with EC number 3.1.26.4 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

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