1ig7: Difference between revisions

Line 1:

[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ig7, resolution 2.20Å" />

'''Msx-1 Homeodomain/DNA Complex Structure'''<br />

==Overview==

The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are, comprised of 60 amino acids that show a high degree of evolutionary, conservation. We have determined the structure of the Msx-1 homeodomain, complexed to DNA at 2.2 A resolution. The structure has an unusually, well-ordered N-terminal arm with a unique trajectory across the minor, groove of the DNA. DNA specificity conferred by bases flanking the core, TAAT sequence is explained by well ordered water-mediated interactions at, Q50. Most interactions seen at the TAAT sequence are typical of the, interactions seen in other homeodomain structures. Comparison of the, Msx-1-HD structure to all other high resolution HD-DNA complex structures, indicate a remarkably well-conserved sphere of hydration between the DNA, and protein in these complexes.

The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.

==About this Structure==

1IG7 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=1IG7 OCA].

1IG7 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=1IG7 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Abate-Shen, C.]]

[[Category: Geiger, J.H.]]

[[Category: Geiger, J H.]]

[[Category: Hovde, S.]]

[[Category: helix-turn-helix]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:22:~~50 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:31 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ig7.gif|left|200px]]<br /><applet load="1ig7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ig7, resolution 2.20&Aring;" />
 '''Msx-1 Homeodomain/DNA Complex Structure'''<br />
 ==Overview==
-The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are, comprised of 60 amino acids that show a high degree of evolutionary, conservation. We have determined the structure of the Msx-1 homeodomain, complexed to DNA at 2.2 A resolution. The structure has an unusually, well-ordered N-terminal arm with a unique trajectory across the minor, groove of the DNA. DNA specificity conferred by bases flanking the core, TAAT sequence is explained by well ordered water-mediated interactions at, Q50. Most interactions seen at the TAAT sequence are typical of the, interactions seen in other homeodomain structures. Comparison of the, Msx-1-HD structure to all other high resolution HD-DNA complex structures, indicate a remarkably well-conserved sphere of hydration between the DNA, and protein in these complexes.
+The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.
 ==About this Structure==
-IG7 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=1IG7 OCA].
+IG7 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=1IG7 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Abate-Shen, C.]]
-[[Category: Geiger, J.H.]]
+[[Category: Geiger, J H.]]
 [[Category: Hovde, S.]]
 [[Category: helix-turn-helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:22:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:31 2008''