1nmv
From Proteopedia
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'''Solution structure of human Pin1'''<br /> | '''Solution structure of human Pin1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http:// | + | 1NMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ww domain group iv]] | [[Category: ww domain group iv]] | ||
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Revision as of 14:29, 15 February 2008
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Solution structure of human Pin1
Overview
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) (hPin1PPIase) with an root mean square deviation of <0.5 A, 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 interface in solution. Interaction, between the two domains of full-length hPin1 is absent when the protein is, dissected into the catalytic and the WW domain. It indicates that the, flexible linker, connecting both domains, promotes binding. By evaluation, of NOESY spectra we can show that the alpha1/beta1 loop, which was, proposed to undergo a large conformational rearrangement in the absence of, sulfate and an Ala-Pro peptide, remained in the closed conformation under, these conditions. Dissociation constants of 0.4 and 2.0 mm for sulfate and, phosphate ions were measured at 12 degrees C by fluorescence spectroscopy., Binding of sulfate prevents hPin1 aggregation and changes surface charges, across the active center and around the reactive and catalytically, essential Cys113. In the absence of sulfate and/or reducing agent this, residue seems to promote aggregation, as observed in hPin1 solutions in, vitro.
About this Structure
1NMV is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding., Bayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P, J Biol Chem. 2003 Jul 11;278(28):26183-93. Epub 2003 Apr 29. PMID:12721297
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