1M4P

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

Summary for 1M4P

• Entry DOI: 10.2210/pdb1m4p/pdb
• Related: 1KPP 1KPQ 1M4Q
• NMR Information: BMRB: 5532
• Descriptor: Tumor Susceptibility gene 101 protein, Gag Polyprotein (2 entities in total)
• Functional Keywords: tsg101 uev domain, virus budding, vacuolar protein sorting, late domain, peptide binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q99816
• Total number of polymer chains: 2
• Total formula weight: 17599.35

Authors

Pornillos, O.,Alam, S.L.,Davis, D.R.,Sundquist, W.I. (deposition date: 2002-07-03, release date: 2002-11-06, Last modification date: 2024-05-22)

Primary citation

Pornillos, O.,Alam, S.L.,Davis, D.R.,Sundquist, W.I.
Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
Nat.Struct.Biol., 9:812-817, 2002

PubMed Abstract: 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.

PubMed: 12379843

Experimental method

SOLUTION NMR