1ihb
From Proteopedia
(New page: 200px<br /> <applet load="1ihb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihb, resolution 1.95Å" /> '''CRYSTAL STRUCTURE O...) |
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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=" | + | |
caption="1ihb, resolution 1.95Å" /> | caption="1ihb, resolution 1.95Å" /> | ||
'''CRYSTAL STRUCTURE OF P18-INK4C(INK6)'''<br /> | '''CRYSTAL STRUCTURE OF P18-INK4C(INK6)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | p18INK4c is a member of a family of INK4 proteins that function to arrest | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: p18-ink4c(ink6)]] | [[Category: p18-ink4c(ink6)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:50 2008'' |
Revision as of 11:11, 21 February 2008
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CRYSTAL STRUCTURE OF P18-INK4C(INK6)
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.
About this Structure
1IHB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CDK4/6 inhibitory protein p18INK4c provides insights into ankyrin-like repeat structure/function and tumor-derived p16INK4 mutations., Venkataramani R, Swaminathan K, Marmorstein R, Nat Struct Biol. 1998 Jan;5(1):74-81. PMID:9437433
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