1a5j: Difference between revisions

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[[Image:1a5j.gif|left|200px]]<br /><applet load="1a5j" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1a5j.gif|left|200px]]<br /><applet load="1a5j" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1a5j" />

'''CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1A5J OCA].

1A5J is a [http://en.wikipedia.org/wiki/Single_protein 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==

Line 13:

[[Category: Gallus gallus]]

[[Category: Single protein]]

[[Category: Carr, M.D.]]

[[Category: Carr, M D.]]

[[Category: Feeney, J.]]

[[Category: Frenkiel, T.A.]]

[[Category: Frenkiel, T A.]]

[[Category: Klempnauer, K.H.]]

[[Category: Klempnauer, K H.]]

[[Category: Mccormick, J.E.]]

[[Category: Mccormick, J E.]]

[[Category: Mcintosh, P.B.]]

[[Category: Mcintosh, P B.]]

[[Category: Wollborn, U.]]

[[Category: dna-binding protein]]

[[Category: protooncogene product]]

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@@ Line 1: / Line 1: @@
-[[Image:1a5j.gif|left|200px]]<br /><applet load="1a5j" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1a5j.gif|left|200px]]<br /><applet load="1a5j" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1a5j" />
 '''CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES'''<br />
 ==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.
+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==
-A5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A5J OCA].
+A5J is a [http://en.wikipedia.org/wiki/Single_protein 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==
@@ Line 13: / Line 13: @@
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
-[[Category: Carr, M.D.]]
+[[Category: Carr, M D.]]
 [[Category: Feeney, J.]]
-[[Category: Frenkiel, T.A.]]
+[[Category: Frenkiel, T A.]]
-[[Category: Klempnauer, K.H.]]
+[[Category: Klempnauer, K H.]]
-[[Category: Mccormick, J.E.]]
+[[Category: Mccormick, J E.]]
-[[Category: Mcintosh, P.B.]]
+[[Category: Mcintosh, P B.]]
 [[Category: Wollborn, U.]]
 [[Category: dna-binding protein]]
 [[Category: protooncogene product]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:37:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:12 2008''