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1idz
From Proteopedia
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'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES''' | '''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES''' | ||
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[[Category: Nakamura, H.]] | [[Category: Nakamura, H.]] | ||
[[Category: Oda, M.]] | [[Category: Oda, M.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:53:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:53, 2 May 2008
STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES
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
1IDZ 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 Page seeded by OCA on Fri May 2 19:53:40 2008
