1ihb: Difference between revisions

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

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

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

caption="1ihb, resolution 1.95Å" />

'''CRYSTAL STRUCTURE OF P18-INK4C(INK6)'''<br />

==Overview==

p18INK4c is a member of a family of INK4 proteins that function to arrest, the G1 to S cell cycle transition by inhibiting the activity of the, cyclin-dependent kinases 4 and 6. The X-ray crystal structure of the human, p18INK4c protein to a resolution of 1.95 A reveals an elongated molecule, comprised of five contiguous 32- or 33-residue ankyrin-like repeat units., Each ankyrin-like repeat contains a beta-strand helix-turn-helix extended, strand beta-strand motif that associates with neighboring motifs through, beta-sheet, and helical bundle interactions. Conserved ankyrin-like repeat, residues function to facilitate the ankyrin repeat fold and the tertiary, interactions between neighboring repeat units. A large percentage of, residues that are conserved among INK4 proteins and that map to positions, of tumor-derived p16INK4 mutations play important roles in protein, stability. A subset of these residues suggest an INK4 binding surface for, the cyclin-dependent kinases 4 and 6. This surface is centered around a, region that shows structural features uncharacteristic of ankyrin-like, repeat units.

p18INK4c is a member of a family of INK4 proteins that function to arrest the G1 to S cell cycle transition by inhibiting the activity of the cyclin-dependent kinases 4 and 6. The X-ray crystal structure of the human p18INK4c protein to a resolution of 1.95 A reveals an elongated molecule comprised of five contiguous 32- or 33-residue ankyrin-like repeat units. Each ankyrin-like repeat contains a beta-strand helix-turn-helix extended strand beta-strand motif that associates with neighboring motifs through beta-sheet, and helical bundle interactions. Conserved ankyrin-like repeat residues function to facilitate the ankyrin repeat fold and the tertiary interactions between neighboring repeat units. A large percentage of residues that are conserved among INK4 proteins and that map to positions of tumor-derived p16INK4 mutations play important roles in protein stability. A subset of these residues suggest an INK4 binding surface for the cyclin-dependent kinases 4 and 6. This surface is centered around a region that shows structural features uncharacteristic of ankyrin-like repeat units.

==About this Structure==

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

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

==Reference==

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[[Category: p18-ink4c(ink6)]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:50 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ihb.gif|left|200px]]<br />
+[[Image:1ihb.gif|left|200px]]<br /><applet load="1ihb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ihb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ihb, resolution 1.95&Aring;" />
 '''CRYSTAL STRUCTURE OF P18-INK4C(INK6)'''<br />
 ==Overview==
-p18INK4c is a member of a family of INK4 proteins that function to arrest, the G1 to S cell cycle transition by inhibiting the activity of the, cyclin-dependent kinases 4 and 6. The X-ray crystal structure of the human, p18INK4c protein to a resolution of 1.95 A reveals an elongated molecule, comprised of five contiguous 32- or 33-residue ankyrin-like repeat units., Each ankyrin-like repeat contains a beta-strand helix-turn-helix extended, strand beta-strand motif that associates with neighboring motifs through, beta-sheet, and helical bundle interactions. Conserved ankyrin-like repeat, residues function to facilitate the ankyrin repeat fold and the tertiary, interactions between neighboring repeat units. A large percentage of, residues that are conserved among INK4 proteins and that map to positions, of tumor-derived p16INK4 mutations play important roles in protein, stability. A subset of these residues suggest an INK4 binding surface for, the cyclin-dependent kinases 4 and 6. This surface is centered around a, region that shows structural features uncharacteristic of ankyrin-like, repeat units.
+p18INK4c is a member of a family of INK4 proteins that function to arrest the G1 to S cell cycle transition by inhibiting the activity of the cyclin-dependent kinases 4 and 6. The X-ray crystal structure of the human p18INK4c protein to a resolution of 1.95 A reveals an elongated molecule comprised of five contiguous 32- or 33-residue ankyrin-like repeat units. Each ankyrin-like repeat contains a beta-strand helix-turn-helix extended strand beta-strand motif that associates with neighboring motifs through beta-sheet, and helical bundle interactions. Conserved ankyrin-like repeat residues function to facilitate the ankyrin repeat fold and the tertiary interactions between neighboring repeat units. A large percentage of residues that are conserved among INK4 proteins and that map to positions of tumor-derived p16INK4 mutations play important roles in protein stability. A subset of these residues suggest an INK4 binding surface for the cyclin-dependent kinases 4 and 6. This surface is centered around a region that shows structural features uncharacteristic of ankyrin-like repeat units.
 ==About this Structure==
-IHB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IHB OCA].
+IHB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHB OCA].
 ==Reference==
@@ Line 22: / Line 21: @@
 [[Category: p18-ink4c(ink6)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:29:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:50 2008''