2k7y Summary


Solution fold of HIV-1 Virus protein U cytoplasmic domain in the presence of DPC micelles

The structure was published by Wittlich, M., Koenig, B.W., Stoldt, M., Schmidt, H., and Willbold, D., in 2009 in a paper entitled "NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2008.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Protein Vpu. This molecule has the UniProt identifier P19554 (VPU_HV1S1)search. The sample contained 45 residues which is < 90% of the natural sequence. Out of 45 residues 45 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Protein Vpu P19554 (39-81) (VPU_HV1S1)search Human immunodeficiency virus type 1 (SF162 ISOLATE)search < 90% 45 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P19554 (39 - 81) Protein Vpu Human immunodeficiency virus type 1 (SF162 ISOLATE)

Chain Sequence family (Pfam)
A Vpu proteinsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P19554) viral release from host cellsearch receptor catabolic processsearch cation channel activitysearch CD4 receptor bindingsearch host cell membranesearch

Chain InterPro annotation
A Vpu proteinsearch Vpu protein cytoplasmic domainsearch