1a5j
From Proteopedia
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| - | [[Image:1a5j.gif|left|200px]] | + | [[Image:1a5j.gif|left|200px]] |
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| - | '''CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1a5j |SIZE=350|CAPTION= <scene name='initialview01'>1a5j</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A5J is a [ | + | 1A5J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A5J OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression., McIntosh PB, Frenkiel TA, Wollborn U, McCormick JE, Klempnauer KH, Feeney J, Carr MD, Biochemistry. 1998 Jul 7;37(27):9619-29. PMID:[http:// | + | Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression., McIntosh PB, Frenkiel TA, Wollborn U, McCormick JE, Klempnauer KH, Feeney J, Carr MD, Biochemistry. 1998 Jul 7;37(27):9619-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9657674 9657674] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[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 09:53:12 2008'' |
Revision as of 07:53, 20 March 2008
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CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES
Overview
Double- and triple-resonance heteronuclear NMR spectroscopy have been used to determine the high-resolution solution structure of the minimal B-Myb DNA-binding domain (B-MybR2R3) and to characterize the specific complex formed with a synthetic DNA fragment corresponding to the Myb target site on the Myb-regulated gene tom-1. B-MybR2R3 is shown to consist of two independent protein domains (R2 and R3) joined by a short linker, which have strikingly different tertiary structures despite significant sequence similarities. In addition, the C-terminal region of B-Myb R2 is confirmed to have a poorly defined structure, reflecting the existence of multiple conformations in slow to intermediate exchange. This contrasts with the tertiary structure reported for c-MybR2R3, in which both R2 and R3 have the same fold and the C-terminal region of R2 forms a stable, well-defined helix [Ogata, K., et al. (1995) Nat. Struct. Biol. 2, 309-320]. The NMR data suggest there are extensive contacts between B-MybR2R3 and its DNA target site in the complex and are consistent with a significant conformational change in the protein on binding to DNA, with one possibility being the formation of a stable helix in the C-terminal region of R2. In addition, conformational heterogeneity identified in R2 of B-MybR2R3 bound to the tom-1-A target site may play an important role in the control of gene expression by Myb proteins.
About this Structure
1A5J is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression., McIntosh PB, Frenkiel TA, Wollborn U, McCormick JE, Klempnauer KH, Feeney J, Carr MD, Biochemistry. 1998 Jul 7;37(27):9619-29. PMID:9657674
Page seeded by OCA on Thu Mar 20 09:53:12 2008
