1mdy: Difference between revisions

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

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

caption="1mdy, resolution 2.800Å" />

'''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''<br />

==Overview==

The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA, complex has been solved and refined at 2.8 A resolution. This structure, proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are, remarkably similar; it helps us understand subtle differences in binding, preferences for these proteins; and it has surprising implications for our, understanding of transcription. Specifically, Ala-114 and Thr-115, which, are required for positive control in the myogenic proteins, are buried at, the protein-DNA interface. These residues are not available for direct, protein-protein contacts, but they may determine the conformation of, Arg-111. Comparisons with Max suggest that the conformation of this, arginine, which is different in the two structures, may play an important, role in myogenic transcription.

The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.

==About this Structure==

1MDY 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA].

1MDY 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=1MDY OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Ma, P.C.M.]]

[[Category: Ma, P C.M.]]

[[Category: Pabo, C.O.]]

[[Category: Pabo, C O.]]

[[Category: Rould, M.A.]]

[[Category: Rould, M A.]]

[[Category: Weintraub, H.]]

[[Category: protein-dna complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 21:21:~~20 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:16 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1mdy.gif|left|200px]]<br /><applet load="1mdy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mdy.gif|left|200px]]<br /><applet load="1mdy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mdy, resolution 2.800&Aring;" />
 '''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''<br />
 ==Overview==
-The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA, complex has been solved and refined at 2.8 A resolution. This structure, proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are, remarkably similar; it helps us understand subtle differences in binding, preferences for these proteins; and it has surprising implications for our, understanding of transcription. Specifically, Ala-114 and Thr-115, which, are required for positive control in the myogenic proteins, are buried at, the protein-DNA interface. These residues are not available for direct, protein-protein contacts, but they may determine the conformation of, Arg-111. Comparisons with Max suggest that the conformation of this, arginine, which is different in the two structures, may play an important, role in myogenic transcription.
+The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.
 ==About this Structure==
-MDY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA].
+MDY 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=1MDY OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Ma, P.C.M.]]
+[[Category: Ma, P C.M.]]
-[[Category: Pabo, C.O.]]
+[[Category: Pabo, C O.]]
-[[Category: Rould, M.A.]]
+[[Category: Rould, M A.]]
 [[Category: Weintraub, H.]]
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:21:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:16 2008''