1idz: Difference between revisions

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[[Image:1idz.jpg|left|200px]]<br /><applet load="1idz" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1idz.jpg|left|200px]]
caption="1idz" />
 
'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES'''<br />
{{Structure
|PDB= 1idz |SIZE=350|CAPTION= <scene name='initialview01'>1idz</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1IDZ 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=1IDZ OCA].  
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8942977 8942977]
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 Feb 21 13:10:52 2008''
''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

File:1idz.jpg


PDB ID 1idz

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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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