1an2: Difference between revisions

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[[Image:1an2.gif|left|200px]]<br />

[[Image:1an2.gif|left|200px]]<br /><applet load="1an2" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1an2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1an2, resolution 2.900Å" />

'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''<br />

==Overview==

The three-dimensional structure of the basic/helix-loop-helix/leucine, zipper domain of the transcription factor Max complexed with DNA has been, determined by X-ray crystallography at 2.9 A resolution. Max binds as a, dimer to its recognition sequence CACGTG by direct contacts between the, alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with, each monomer containing two alpha-helical segments separated by a loop., The two alpha-helical segments are composed of the basic region plus helix, 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the, leucine repeat forms a parallel coiled coil.

The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.

==About this Structure==

1AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].

1AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].

==Reference==

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[[Category: ]]

[[Category: Single protein]]

[[Category: Amare, A.R.Ferre-D.]]

[[Category: Amare, A R.Ferre-D.]]

[[Category: Burley, S.K.]]

[[Category: Burley, S K.]]

[[Category: Prendergast, G.C.]]

[[Category: Prendergast, G C.]]

[[Category: Ziff, E.B.]]

[[Category: Ziff, E B.]]

[[Category: double helix]]

[[Category: protein-dna complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 16~~:00:~~05 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1an2.gif|left|200px]]<br />
+[[Image:1an2.gif|left|200px]]<br /><applet load="1an2" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1an2" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1an2, resolution 2.900&Aring;" />
 '''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''<br />
 ==Overview==
-The three-dimensional structure of the basic/helix-loop-helix/leucine, zipper domain of the transcription factor Max complexed with DNA has been, determined by X-ray crystallography at 2.9 A resolution. Max binds as a, dimer to its recognition sequence CACGTG by direct contacts between the, alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with, each monomer containing two alpha-helical segments separated by a loop., The two alpha-helical segments are composed of the basic region plus helix, 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the, leucine repeat forms a parallel coiled coil.
+The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
 ==About this Structure==
-AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].
+AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: ]]
 [[Category: Single protein]]
-[[Category: Amare, A.R.Ferre-D.]]
+[[Category: Amare, A R.Ferre-D.]]
-[[Category: Burley, S.K.]]
+[[Category: Burley, S K.]]
-[[Category: Prendergast, G.C.]]
+[[Category: Prendergast, G C.]]
-[[Category: Ziff, E.B.]]
+[[Category: Ziff, E B.]]
 [[Category: double helix]]
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:00:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:22 2008''