1idz: Difference between revisions
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'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1idz |SIZE=350|CAPTION= <scene name='initialview01'>1idz</scene> | |||
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'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IDZ is a [ | 1IDZ is a [[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=1IDZ OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8942977 8942977] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protooncogene product]] | [[Category: protooncogene product]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:06 2008'' |
Revision as of 12:49, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
1IDZ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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