2pea
From Proteopedia
(New page: 200px<br /> <applet load="2pea" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pea" /> '''NMR Based Structure of the Closed Conformat...) |
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'''NMR Based Structure of the Closed Conformation of LYS48-Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tensor from NMR Relaxation Measurements'''<br /> | '''NMR Based Structure of the Closed Conformation of LYS48-Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tensor from NMR Relaxation Measurements'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2PEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:35:52 2008'' |
Revision as of 12:35, 23 January 2008
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NMR Based Structure of the Closed Conformation of LYS48-Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tensor from NMR Relaxation Measurements
Overview
We present a simple and robust approach that uses the overall rotational, diffusion tensor as a structural constraint for domain positioning in, multidomain proteins and protein-protein complexes. This method offers the, possibility to use NMR relaxation data for detailed structure, characterization of such systems provided the structures of individual, domains are available. The proposed approach extends the concept of using, long-range information contained in the overall rotational diffusion, tensor. In contrast to the existing approaches, we use both the principal, axes and principal values of protein's rotational diffusion tensor to, determine not only the orientation but also the relative positioning of, the individual domains in a protein. This is achieved by finding the, domain arrangement in a molecule that provides the best possible agreement, with all components of the overall rotational diffusion tensor derived, from experimental data. The accuracy of the proposed approach is, demonstrated for two protein systems with known domain arrangement and, parameters of the overall tumbling: the HIV-1 protease homodimer and, Maltose Binding Protein. The accuracy of the method and its sensitivity to, domain positioning are also tested using computer-generated data for three, protein complexes, for which the experimental diffusion tensors are not, available. In addition, the proposed method is applied here to determine, for the first time, the structure of both open and closed conformations of, a Lys48-linked diubiquitin chain, where domain motions render impossible, accurate structure determination by other methods. The proposed method, opens new avenues for improving structure characterization of proteins in, solution.
About this Structure
2PEA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural assembly of multidomain proteins and protein complexes guided by the overall rotational diffusion tensor., Ryabov Y, Fushman D, J Am Chem Soc. 2007 Jun 27;129(25):7894-902. Epub 2007 Jun 6. PMID:17550252
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