PR - Protease - Retropepsin

HIV PR is an aspartyl protease and is required for cleavage of Gag, Gag-Pol, Pol and Nef precursors.




PDB-1AAQ: HIV-1 (isolate UNKNOWN) Protease with peptide - produced using SwissModel/SPDBV/POVray
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ViralZone:HIV-1
PDB: 1AAQ (HIV-1 Protease)
SwissProt: P04585 (HIV-1 HXB2 POL)
Chime Tutorial: Online Macromolecular Museum
Los Alamos HIV structure DB: Protease
EMBL: K03455 [EMBL/GenBank/DDBJ]
BioAfrica: Pol Protein Data Mining Tool


Isoforms:

  • p15 (99 amino acids)

Cleavage site:


Localization:

  • Virion

Function:

  • Viral enzyme
  • Protease activity initiates virion maturation
  • Processes Gag and Gag-pol polyproteins into mature chains

Additional Information:

  • Protease is an aspartyl protease
  • Protease functions while in a homodimer

Genomic Location: [TOP]

Reference Sequences:

HIV-1 (HXB2):

          10         20         30         40         50         60         70 
| | | | | | |
PQVTLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK
80 90 99
| | |
AIGTVLVGPT PVNIIGRNLL TQIGCTLNF
[download in fasta format]

Length: 99 amino acids (residues 57 to 155)
Molecular Weight: 10779 Da
Theoretical pI: 8.83


Protein Domains/Folds/Motifs: [TOP]

InterPro signature for active site Aspartic Peptidase - IPR001969
InterPro signature for Retrovirus Peptidase A2A - IPR001995
InterPro signature for Aspartic Peptidase Family - IPR009007


Secondary Structure prediction:

Antigenic Sites - EMBOSS:


Predicted Motifs: Printer-friendly version

N-glycosylation:
N-myristoylation:
Amidation:
Protein kinase C:
Casein kinase II:
Tyrosine kinase:
cAMP / cGMP kinase:
Cell attachment motif:
Asp Protease motif:
Asp Prot Retro motif:
Cysteine-rich Region:
Tryptophan-rich Region:
Zinc-finger CCHC motif:
Leucine Zipper motif:

Protein-Protein Interactions: [TOP]



Primary and Secondary Database Entries: [TOP]

Identifiers:

ViralZone: HIV-1
PDB/MMDB: Search for HIV-1 & Protease

SwissProt: P04585 (HIV-1 HXB2 POL)
EC: 3.4.23.16
EMBL: K03455; AAB50259.1 [EMBL/GenBank/DDBJ]

PIR: UNKNOWN
HIV: K03455; UNKNOWN$HXB2
InterPro: IPR001969 / IPR001995
Pfam: PF00558;UNKNOWN
Prints: none
ProDom: PD186096 (1 - 16)
SCOP: SSF50630 Acid protease
BLOCKS: P04585
Prosite: P04585
ProtoNet: P04585
ProtoMap: P04585
PRESAGE: P04585
Database of Interacting Proteins: P04585
ModBase: P04585
Swiss-2DPAGE: 2D gel

BioAfrica Tools:
- Pol Protein Data Mining Tool provides real-time analysis of HIV-1 Pol isolates
- HIV Structure BLAST searches for similar HIV sequences that have known structures
- HIV Proteomics Resource contains protein sequence and structure analysis tools

Reviews and References: [TOP]

Cite the resource by citing the following paper:
Doherty R et al. BioAfrica's HIV-1 Proteomics Resource: Combining protein data with bioinformatics tools. Retrovirology (2005), 9;2(1):18.

1 - HIV Sequence Compendium 2000
Kuiken CL, Foley B, Hahn B, Korber B, Marx PA, McCutchan F, Mellors JW, Mullins JI, Sodroski J, Wolinksy S.
Theoretical Biol. & Biophys. Group, Los Alamos Nat Lab, LA-UR 01-3860 [Read it online: Compendium]
2 - Retroviruses
Coffin JM, Hughes SH, Varmus HE.
CD-ROM ed. (2002) Cold Spring Harbor Laboratory Press [Read it online: NCBI Bookshelf]
3 - Molecular Characteristics of HIV-1 Subtype C Viruses from KwaZulu-Natal, South Africa:
Implications for Vaccine and Antiretroviral Control Strategies.
Gordon M, De Oliveira T, Bishop K, Coovadia HM, Madurai L, Engelbrecht S, Janse van Rensburg E, Mosam A, Smith A, Cassol S.
Journal of Virology 77(4): 2587-2599 (2003) [pubmed: 12551997]
4 - An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses
and spread of infection.
Ashorn P, McQuade TJ, Thaisrivongs S.
Proc Natl Acad Sci USA 87: 7472-7476 (1990) [pubmed: 2217178]
5 - Crystal structure of a retroviral protease proves relationship to aspartic protease family.
Miller M, Jaskolski M, Rao JK.
Nature 337: 576-579 (1989) [pubmed: 2536902]
6 - Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.
Navia MA, Fitzgerald PM, McKeever BM.
Nature 337: 615-620 (1989) [pubmed: 2645523]
7 - [HIV Protease Drug Design - Review] Aspartic proteinases in disease: a structural perspective.
Cooper JB.
Curr Drug Targets 3(2):155-173 (2002) [pubmed: 11958298]
8 - [Website] HIV Drug Resistance Database
Stanford
Website: http://hivdb.stanford.edu
9 - [Website] HIV Drug Resistance Database
Los Alamos National Labs
Website: http://resdb.lanl.gov/Resist_DB/default.htm
10 - [Website] HIVdb: a database of the structures of human immunodeficiency virus protease.
NIST
Website: http://srdata.nist.gov/hivdb/



Page last updated by Tulio de Oliveira.