J. Biol. Chem.

Bayer, E.
Goettsch, S.
Mueller, J.
Griewel, B.
Guiberman, E.
Mayr, L.
Bayer, P.

Publication date

July 2003

Abstract

The peptidyl-prolyl cis/trans isomerase hPin1 is a phosphorylation-dependent regulatory enzyme whose substrates are proteins involved in regulation of cell cycle, transcription, Alzheimer's disease, and cancer pathogenesis. We have determined the solution structure of the two domain protein hPin1-(1-163) and its separately expressed PPIase domain ( 50-163) ( hPin1(PPIase)) with an root mean square deviation of <0.5 &ANGS; over backbone atoms using NMR. Domain organization of hPin1 differs from that observed in structures solved by x-ray crystallography. Whereas PPIase and WW domain are tightly packed onto each other and share a common binding interface in crystals, our NMR-based data revealed only weak interaction of both domains at their i...

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J. Biol. Chem.

Abstract

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J. Biol. Chem.

Abstract

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