2o6v

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(New page: 200px<br /> <applet load="2o6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o6v, resolution 2.2&Aring;" /> '''Crystal structure an...)
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<applet load="2o6v" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2o6v, resolution 2.2&Aring;" />
caption="2o6v, resolution 2.2&Aring;" />
'''Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH'''<br />
'''Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH'''<br />
==Overview==
==Overview==
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Ubiquitin modification of proteins is used as a signal in many cellular, processes. Lysine side-chains can be modified by a single ubiquitin or by, a polyubiquitin chain, which is defined by an isopeptide bond between the, C terminus of one ubiquitin and a specific lysine in a neighboring, ubiquitin. Polyubiquitin conformations that result from different lysine, linkages presumably differentiate their roles and ability to bind specific, targets and enzymes. However, conflicting results have been obtained, regarding the precise conformation of Lys48-linked tetraubiquitin. We, report the crystal structure of Lys48-linked tetraubiquitin at, near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit, show the complete connectivity of the chain and the molecular details of, the interactions. This tetraubiquitin conformation is consistent with our, NMR data as well as with previous studies of diubiquitin and, tetraubiquitin in solution at neutral pH. The structure provides a basis, for understanding Lys48-linked polyubiquitin recognition under, physiological conditions.
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Ubiquitin modification of proteins is used as a signal in many cellular processes. Lysine side-chains can be modified by a single ubiquitin or by a polyubiquitin chain, which is defined by an isopeptide bond between the C terminus of one ubiquitin and a specific lysine in a neighboring ubiquitin. Polyubiquitin conformations that result from different lysine linkages presumably differentiate their roles and ability to bind specific targets and enzymes. However, conflicting results have been obtained regarding the precise conformation of Lys48-linked tetraubiquitin. We report the crystal structure of Lys48-linked tetraubiquitin at near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit show the complete connectivity of the chain and the molecular details of the interactions. This tetraubiquitin conformation is consistent with our NMR data as well as with previous studies of diubiquitin and tetraubiquitin in solution at neutral pH. The structure provides a basis for understanding Lys48-linked polyubiquitin recognition under physiological conditions.
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==Disease==
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Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]]
==About this Structure==
==About this Structure==
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2O6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O6V OCA].
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2O6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O6V OCA].
==Reference==
==Reference==
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Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH., Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C, J Mol Biol. 2007 Mar 16;367(1):204-11. Epub 2006 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17240395 17240395]
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Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH., Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C, J Mol Biol. 2007 Mar 16;367(1):204-11. Epub 2006 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17240395 17240395]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Eddins, M.J.]]
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[[Category: Eddins, M J.]]
[[Category: MES]]
[[Category: MES]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: ubiquitin]]
[[Category: ubiquitin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:07:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:11 2008''

Revision as of 16:15, 21 February 2008


2o6v, resolution 2.2Å

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Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

Contents

Overview

Ubiquitin modification of proteins is used as a signal in many cellular processes. Lysine side-chains can be modified by a single ubiquitin or by a polyubiquitin chain, which is defined by an isopeptide bond between the C terminus of one ubiquitin and a specific lysine in a neighboring ubiquitin. Polyubiquitin conformations that result from different lysine linkages presumably differentiate their roles and ability to bind specific targets and enzymes. However, conflicting results have been obtained regarding the precise conformation of Lys48-linked tetraubiquitin. We report the crystal structure of Lys48-linked tetraubiquitin at near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit show the complete connectivity of the chain and the molecular details of the interactions. This tetraubiquitin conformation is consistent with our NMR data as well as with previous studies of diubiquitin and tetraubiquitin in solution at neutral pH. The structure provides a basis for understanding Lys48-linked polyubiquitin recognition under physiological conditions.

Disease

Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]

About this Structure

2O6V is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH., Eddins MJ, Varadan R, Fushman D, Pickart CM, Wolberger C, J Mol Biol. 2007 Mar 16;367(1):204-11. Epub 2006 Dec 29. PMID:17240395

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