1jow: Difference between revisions

Revision as of 14:25, 21 February 2008

Crystal structure of a complex of human CDK6 and a viral cyclin

OverviewOverview

Cyclin from herpesvirus saimiri (Vcyclin) preferentially forms complexes with cyclin-dependent kinase 6 (CDK6) from primate host cells. These complexes show higher kinase activity than host cell CDKs in complex with cellular cyclins and are resistant to cyclin-dependent inhibitory proteins (CDKIs). The crystal structure of human CDK6--Vcyclin in an active state was determined to 3.1 A resolution to better understand the structural basis of CDK6 activation by viral cyclins. The unphosphorylated CDK6 in complex with Vcyclin has many features characteristic of cyclinA-activated, phosphorylated CDK2. There are, however, differences in the conformation at the tip of the T-loop and its interactions with Vcyclin. Residues in the N-terminal extension of Vcyclin wrap around the tip of the CDK6 T-loop and form a short beta-sheet with the T-loop backbone. These interactions lead to a 20% larger buried surface in the CDK6--Vcyclin interface than in the CDK2--cyclinA complex and are probably largely responsible for the specificity of Vcyclin for CDK6 and resistance of the complex to inhibition by INK-type CDKIs.

About this StructureAbout this Structure

1JOW is a Protein complex structure of sequences from Homo sapiens and Saimiriine herpesvirus 3. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for CDK6 activation by a virus-encoded cyclin., Schulze-Gahmen U, Kim SH, Nat Struct Biol. 2002 Mar;9(3):177-81. PMID:11828325

Page seeded by OCA on Thu Feb 21 13:25:02 2008

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OCA

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-[[Image:1jow.gif|left|200px]]<br />
+[[Image:1jow.gif|left|200px]]<br /><applet load="1jow" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1jow" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1jow, resolution 3.10&Aring;" />
 '''Crystal structure of a complex of human CDK6 and a viral cyclin'''<br />
 ==Overview==
-Cyclin from herpesvirus saimiri (Vcyclin) preferentially forms complexes, with cyclin-dependent kinase 6 (CDK6) from primate host cells. These, complexes show higher kinase activity than host cell CDKs in complex with, cellular cyclins and are resistant to cyclin-dependent inhibitory proteins, (CDKIs). The crystal structure of human CDK6--Vcyclin in an active state, was determined to 3.1 A resolution to better understand the structural, basis of CDK6 activation by viral cyclins. The unphosphorylated CDK6 in, complex with Vcyclin has many features characteristic of, cyclinA-activated, phosphorylated CDK2. There are, however, differences in, the conformation at the tip of the T-loop and its interactions with, Vcyclin. Residues in the N-terminal extension of Vcyclin wrap around the, tip of the CDK6 T-loop and form a short beta-sheet with the T-loop, backbone. These interactions lead to a 20% larger buried surface in the, CDK6--Vcyclin interface than in the CDK2--cyclinA complex and are probably, largely responsible for the specificity of Vcyclin for CDK6 and resistance, of the complex to inhibition by INK-type CDKIs.
+Cyclin from herpesvirus saimiri (Vcyclin) preferentially forms complexes with cyclin-dependent kinase 6 (CDK6) from primate host cells. These complexes show higher kinase activity than host cell CDKs in complex with cellular cyclins and are resistant to cyclin-dependent inhibitory proteins (CDKIs). The crystal structure of human CDK6--Vcyclin in an active state was determined to 3.1 A resolution to better understand the structural basis of CDK6 activation by viral cyclins. The unphosphorylated CDK6 in complex with Vcyclin has many features characteristic of cyclinA-activated, phosphorylated CDK2. There are, however, differences in the conformation at the tip of the T-loop and its interactions with Vcyclin. Residues in the N-terminal extension of Vcyclin wrap around the tip of the CDK6 T-loop and form a short beta-sheet with the T-loop backbone. These interactions lead to a 20% larger buried surface in the CDK6--Vcyclin interface than in the CDK2--cyclinA complex and are probably largely responsible for the specificity of Vcyclin for CDK6 and resistance of the complex to inhibition by INK-type CDKIs.
 ==About this Structure==
-JOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saimiriine_herpesvirus_3 Saimiriine herpesvirus 3]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JOW OCA].
+JOW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saimiriine_herpesvirus_3 Saimiriine herpesvirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOW OCA].
 ==Reference==
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 [[Category: Protein complex]]
 [[Category: Saimiriine herpesvirus 3]]
-[[Category: Kim, S.H.]]
+[[Category: Kim, S H.]]
 [[Category: Schulze-Gahmen, U.]]
 [[Category: cdk-cyclin complex]]
 [[Category: cyclin fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:43:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:02 2008''