1fpz | pdb_00001fpz
From Proteopedia
CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE
Template:ABSTRACT PUBMED 11463386
Disease
[CDKN3_HUMAN] Defects in CDKN3 are found in patients with hepatocellular carcinoma (HCC) [MIM:114550].[1]
Function
[CDKN3_HUMAN] May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner.[2][3][4]
About this Structure
1fpz is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell. 2001 Mar;7(3):615-26. PMID:11463386
- ↑ Yeh CT, Lu SC, Chen TC, Peng CY, Liaw YF. Aberrant transcripts of the cyclin-dependent kinase-associated protein phosphatase in hepatocellular carcinoma. Cancer Res. 2000 Sep 1;60(17):4697-700. PMID:10987270
- ↑ Gyuris J, Golemis E, Chertkov H, Brent R. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell. 1993 Nov 19;75(4):791-803. PMID:8242750
- ↑ Hannon GJ, Casso D, Beach D. KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases. Proc Natl Acad Sci U S A. 1994 Mar 1;91(5):1731-5. PMID:8127873
- ↑ Poon RY, Hunter T. Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science. 1995 Oct 6;270(5233):90-3. PMID:7569954
