1idy
From Proteopedia
(New page: 200px<br /><applet load="1idy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idy" /> '''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, ...) |
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| - | [[Image:1idy.gif|left|200px]]<br /><applet load="1idy" size=" | + | [[Image:1idy.gif|left|200px]]<br /><applet load="1idy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1idy" /> | caption="1idy" /> | ||
'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A small globular protein, the third repeat of the c-Myb DNA-binding | + | A small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1IDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1IDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protooncogene product]] | [[Category: protooncogene product]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:54 2008'' |
Revision as of 11:10, 21 February 2008
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STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
A small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure.
About this Structure
1IDY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy., Furukawa K, Oda M, Nakamura H, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13583-8. PMID:8942977
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