1m4p: Difference between revisions

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==Overview==
==Overview==
The structural proteins of HIV and Ebola display PTAP peptide motifs, (termed 'late domains') that recruit the human protein Tsg101 to, facilitate virus budding. Here we present the solution structure of the, UEV (ubiquitin E2 variant) binding domain of Tsg101 in complex with a PTAP, peptide that spans the late domain of HIV-1 p6(Gag). The UEV domain of, Tsg101 resembles E2 ubiquitin-conjugating enzymes, and the PTAP peptide, binds in a bifurcated groove above the vestigial enzyme active site. Each, PTAP residue makes important contacts, and the Ala 9-Pro 10 dipeptide, binds in a deep pocket of the UEV domain that resembles the X-Pro binding, pockets of SH3 and WW domains. The structure reveals the molecular basis, of HIV PTAP late domain function and represents an attractive starting, point for the design of novel inhibitors of virus budding.
The structural proteins of HIV and Ebola display PTAP peptide motifs (termed 'late domains') that recruit the human protein Tsg101 to facilitate virus budding. Here we present the solution structure of the UEV (ubiquitin E2 variant) binding domain of Tsg101 in complex with a PTAP peptide that spans the late domain of HIV-1 p6(Gag). The UEV domain of Tsg101 resembles E2 ubiquitin-conjugating enzymes, and the PTAP peptide binds in a bifurcated groove above the vestigial enzyme active site. Each PTAP residue makes important contacts, and the Ala 9-Pro 10 dipeptide binds in a deep pocket of the UEV domain that resembles the X-Pro binding pockets of SH3 and WW domains. The structure reveals the molecular basis of HIV PTAP late domain function and represents an attractive starting point for the design of novel inhibitors of virus budding.


==Disease==
==Disease==
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[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Alam, S.L.]]
[[Category: Alam, S L.]]
[[Category: Davis, D.R.]]
[[Category: Davis, D R.]]
[[Category: Pornillos, O.]]
[[Category: Pornillos, O.]]
[[Category: Sundquist, W.I.]]
[[Category: Sundquist, W I.]]
[[Category: late domain]]
[[Category: late domain]]
[[Category: tsg101 uev domain]]
[[Category: tsg101 uev domain]]
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[[Category: virus budding]]
[[Category: virus budding]]


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Revision as of 14:51, 21 February 2008

File:1m4p.jpg


1m4p

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Structure of the Tsg101 UEV domain in complex with a HIV-1 PTAP "late domain" peptide, DYANA Ensemble

OverviewOverview

The structural proteins of HIV and Ebola display PTAP peptide motifs (termed 'late domains') that recruit the human protein Tsg101 to facilitate virus budding. Here we present the solution structure of the UEV (ubiquitin E2 variant) binding domain of Tsg101 in complex with a PTAP peptide that spans the late domain of HIV-1 p6(Gag). The UEV domain of Tsg101 resembles E2 ubiquitin-conjugating enzymes, and the PTAP peptide binds in a bifurcated groove above the vestigial enzyme active site. Each PTAP residue makes important contacts, and the Ala 9-Pro 10 dipeptide binds in a deep pocket of the UEV domain that resembles the X-Pro binding pockets of SH3 and WW domains. The structure reveals the molecular basis of HIV PTAP late domain function and represents an attractive starting point for the design of novel inhibitors of virus budding.

DiseaseDisease

Known disease associated with this structure: Breast cancer OMIM:[601387]

About this StructureAbout this Structure

1M4P is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein., Pornillos O, Alam SL, Davis DR, Sundquist WI, Nat Struct Biol. 2002 Nov;9(11):812-7. PMID:12379843

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