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- PDB-1rpv: HIV-1 REV PROTEIN (RESIDUES 34-50) -

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Basic information

Entry
Database: PDB / ID: 1rpv
TitleHIV-1 REV PROTEIN (RESIDUES 34-50)
ComponentsHIV-1 REV PROTEIN
KeywordsTRANSCRIPTION REGULATION PROTEIN / HUMAN IMMUNODEFICIENCY VIRUS-1 / REV RESPONSE ELEMENT
Function / homology
Function and homology information


protein localization to nucleoplasm / host cell nucleolus / mRNA transport / viral process / host cell cytoplasm / DNA-binding transcription factor activity / RNA binding
Similarity search - Function
Anti-repression trans-activator protein, REV protein / REV protein (anti-repression trans-activator protein)
Similarity search - Domain/homology
Protein Rev / Protein Rev
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1
MethodSOLUTION NMR
AuthorsScanlon, M.J. / Fairlie, D.P. / Craik, D.J. / Englebretsen, D.R. / West, M.L.
Citation
Journal: Biochemistry / Year: 1995
Title: NMR solution structure of the RNA-binding peptide from human immunodeficiency virus (type 1) Rev.
Authors: Scanlon, M.J. / Fairlie, D.P. / Craik, D.J. / Englebretsen, D.R. / West, M.L.
#1: Journal: Biochemistry / Year: 1994
Title: 1H NMR Studies of the High-Affinity Rev Binding Site of the Rev Responsive Element of HIV-1 Mrna: Base Pairing in the Core Binding Element
Authors: Peterson, R.D. / Bartel, D.P. / Szostak, J.W. / Horvath, S.J. / Feigon, J.
#2: Journal: Biochemistry / Year: 1994
Title: Binding of an HIV Rev Peptide to Rev Responsive Element RNA Induces Formation of Purine-Purine Base Pairs
Authors: Battiste, J.L. / Tan, R. / Frankel, A.D. / Williamson, J.R.
#3: Journal: Nat.Struct.Biol. / Year: 1994
Title: A Three-Dimensional Model of the Rev Binding Element of HIV-1 Derived from Analyses of Aptamers
Authors: Leclerc, F. / Cedergren, R. / Ellington, A.D.
#4: Journal: Cell(Cambridge,Mass.) / Year: 1993
Title: RNA Recognition by an Isolated Alpha Helix
Authors: Tan, R. / Chen, L. / Buettner, J.A. / Hudson, D. / Frankel, A.D.
#5: Journal: Nature / Year: 1989
Title: Specific Binding of HIV-1 Recombinant Rev Protein to the Rev-Responsive Element in Vitro
Authors: Daly, T.J. / Cook, K.S. / Gray, G.S. / Maione, T.E. / Rusche, J.R.
History
DepositionMay 4, 1995Processing site: BNL
Revision 1.0Oct 15, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HIV-1 REV PROTEIN


Theoretical massNumber of molelcules
Total (without water)2,4021
Polymers2,4021
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein/peptide HIV-1 REV PROTEIN


Mass: 2401.747 Da / Num. of mol.: 1 / Mutation: R42A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 (CLONE 12)
Genus: Lentivirus / Species: Human immunodeficiency virus 1 / References: UniProt: P12485, UniProt: P04325*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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