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1fpz

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[[Image:1fpz.png|left|200px]]
 
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{{STRUCTURE_1fpz| PDB=1fpz | SCENE= }}
{{STRUCTURE_1fpz| PDB=1fpz | SCENE= }}
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===CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE===
===CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE===
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{{ABSTRACT_PUBMED_11463386}}
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{{ABSTRACT_PUBMED_11463386}}
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==Disease==
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[[http://www.uniprot.org/uniprot/CDKN3_HUMAN CDKN3_HUMAN]] Defects in CDKN3 are found in patients with hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]].<ref>PMID:10987270</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/CDKN3_HUMAN 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.<ref>PMID:8242750</ref><ref>PMID:8127873</ref><ref>PMID:7569954</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:011463386</ref><references group="xtra"/>
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<ref group="xtra">PMID:011463386</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]

Revision as of 07:11, 25 March 2013

Template:STRUCTURE 1fpz

Contents

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
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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

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