Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
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Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
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Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
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Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
The 2 . 6 Angstrom crystal structure for human cyclin dependent kinase 2 ( CDK 2 ) in complex with CksHs 1 , a human homolog of essential yeast cell cycle regulatory proteins suc 1 and Cks 1 , reveals that CksHs 1 binds via all four beta strands to the kinase C terminal lobe . ^^^
Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
This response was specific to Cdk 2 binding ; in contrast , binding of Skp 2 , a ligand unique to human Cks 1 , did not alter the dynamic behavior . ^^^ Short time ( < 5 ns ) molecular dynamics simulations indicate that residues of Cks 1 that form the binding site for phosphorylated ligands are considerably more flexible in the free form of Cks 1 than they are in the Cdk 2 Cks1 complex . ^^^ A cooperative interaction between Cdk 2 and Cks 1 is suggested , which reduces the configurational entropy of Cks 1 and therefore facilitates phosphoprotein binding . ^^^
Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
The structure and biochemical data support the proposed model that Cdk 2 cyclin A contributes to the recruitment of p 27 ( Kip 1 ) to the SCF ( Skp 2 ) Cks 1 complex . . ^^^
Interacting proteins: P61024 and P24941 Pubmed SVM Score :0.0
For analyzing relationships of CKS with cell proliferation and / or with differentiation , we investigated the expression of ckshs 1 and ckshs 2 in normal and malignant human lymphoid cells . ckshs 1 and ckshs 2 expression appeared to be related to cell proliferation : ( 1 ) mRNAs increased with stimulation of normal peripheral blood lymphocytes , and from the G 1 to the SG2M phase in elutriated cells ; ( 2 ) P 9 proteins were also induced by lymphocyte stimulation and were localized in nucleus where phosphorylated forms of CDK 1 were also found ; ( 3 ) in vitro , the phosphorylated forms of CDK 1 and CDK 2 were preferentially linked to CKS . ^^^