2f0r: Difference between revisions
New page: left|200px<br /> <applet load="2f0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f0r, resolution 2.26Å" /> '''Crystallographic st... |
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[[Image:2f0r.gif|left|200px]]<br /> | [[Image:2f0r.gif|left|200px]]<br /><applet load="2f0r" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2f0r, resolution 2.26Å" /> | caption="2f0r, resolution 2.26Å" /> | ||
'''Crystallographic structure of human Tsg101 UEV domain'''<br /> | '''Crystallographic structure of human Tsg101 UEV domain'''<br /> | ||
==Overview== | ==Overview== | ||
The UEV domain of the TSG101 protein functions in the vacuolar | The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2F0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2F0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F0R OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Camara-Artigas, A.]] | [[Category: Camara-Artigas, A.]] | ||
[[Category: Luque, I.]] | [[Category: Luque, I.]] | ||
[[Category: Martinez, J | [[Category: Martinez, J C.]] | ||
[[Category: Mateo, P | [[Category: Mateo, P L.]] | ||
[[Category: Palencia, A]] | [[Category: Palencia, A]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: tsg101]] | [[Category: tsg101]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:30 2008'' | ||
Revision as of 18:16, 21 February 2008
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Crystallographic structure of human Tsg101 UEV domain
OverviewOverview
The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition.
DiseaseDisease
Known disease associated with this structure: Breast cancer OMIM:[601387]
About this StructureAbout this Structure
2F0R is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human TSG101 UEV domain., Palencia A, Martinez JC, Mateo PL, Luque I, Camara-Artigas A, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):458-64. Epub 2006, Mar 18. PMID:16552148
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