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PDBsum entry 2f0r
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Unknown function
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PDB id
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2f0r
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References listed in PDB file
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Key reference
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Title
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Structure of human tsg101 uev domain.
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Authors
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A.Palencia,
J.C.Martinez,
P.L.Mateo,
I.Luque,
A.Camara-Artigas.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
458-464.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Ribbon representation of the crystal structure of the human TSG101 UEV domain. [beta]
-Strands are coloured yellow and labelled S1-S5 and [alpha] -helices are coloured red
and labelled H1-H3. Loops important for ubiquitin recognition are labelled `lip' and
`tongue'.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
458-464)
copyright 2006.
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