Gag-Pol polyprotein

Details

Name
Gag-Pol polyprotein
Kind
protein
Synonyms
  • Pr160Gag-Pol
Gene Name
gag-pol
UniProtKB Entry
P04587Swiss-Prot
Organism
HIV-1
NCBI Taxonomy ID
11682
Amino acid sequence
>lcl|BSEQ0007855|Gag-Pol polyprotein
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI
LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA
DTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT
PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT
STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF
YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA
RVLAEAMSQVTNSTTIMMQRGNFRNQRKIVKCFNCGKEGHIARNCKAPRKKGCWKCGKEG
HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGR
DNNSPSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG
RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP
ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVF
AIKKKDSTKWRKLVDFRELNRRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLD
EDFRKYTAFTIPSINNETPGSGYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIY
QYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTI
QPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL
ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAH
TNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPP
LVKLWYQLEKEPIVGAETFYVDGAASRETKLGKAGYVTNRGRQKVVTLTHTTNQKTELQA
IHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKG
IGGNEQVDKLVSAGIRKILFLDGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCD
KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFL
LKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKI
IGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQ
NFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCV
ASRQDED
Number of residues
1447
Molecular Weight
163264.37
Theoretical pI
9.07
GO Classification
Functions
aspartic-type endopeptidase activity / DNA binding / DNA-directed DNA polymerase activity / exoribonuclease H activity / lipid binding / RNA binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / structural molecule activity / zinc ion binding
Processes
DNA integration / DNA recombination / establishment of integrated proviral latency / induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / suppression by virus of host gene expression / viral entry into host cell / viral penetration into host nucleus / viral release from host cell
Components
host cell nucleus / host cell plasma membrane / host multivesicular body / viral nucleocapsid / virion membrane
General Function
Gag-Pol polyprotein Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation.
Specific Function
aspartic-type endopeptidase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Host cell membrane
Gene sequence
>lcl|BSEQ0007854|1539 bp
GAGTACGCCAAAAATTTTGACTAGCGGAGGCTAGAAGGAGAGAGATGGGTGCGAGAGCGT
CAGTATTAAGCGGGGGAGAATTAGATCGATGGGAAAAAATTCGGTTAAGGCCAGGGGGAA
AGAAAAAATATAAATTAAAACATATAGTATGGGCAAGCAGGGAGCTAGAACGATTCGCAG
TTAATCCTGGCCTGTTAGAAACATCAGAAGGCTGTAGACAAATACTGGGACAGCTACAAC
CATCCCTTCAGACAGGATCAGAAGAACTTAGATCATTATATAATACAGTAGCAACCCTCT
ATTGTGTGCATCAAAGGATAGAGATAAAAGACACCAAGGAAGCTTTAGACAAGATAGAGG
AAGAGCAAAACAAAAGTAAGAAAAAAGCACAGCAAGCAGCAGCTGACACAGGACACAGCA
GTCAGGTCAGCCAAAATTACCCTATAGTGCAGAACATCCAGGGGCAAATGGTACATCAGG
CCATATCACCTAGAACTTTAAATGCATGGGTAAAAGTAGTAGAAGAGAAGGCTTTCAGCC
CAGAAGTGATACCCATGTTTTCAGCATTATCAGAAGGAGCCACCCCACAAGATTTAAACA
CCATGCTAAACACAGTGGGGGGACATCAAGCAGCCATGCAAATGTTAAAAGAGACCATCA
ATGAGGAAGCTGCAGAATGGGATAGAGTGCATCCAGTGCATGCAGGGCCTATCGCACCAG
GCCAGATGAGAGAACCAAGGGGAAGTGACATAGCAGGAACTACTAGTACCCTTCAGGAAC
AAATAGGATGGATGACAAATAATCCACCTATCCCAGTAGGAGAAATTTATAAAAGATGGA
TAATCCTGGGATTAAATAAAATAGTAAGGATGTATAGTCCTACCAGCATTCTGGACATAA
GACAAGGACCAAAGGAACCCTTTAGAGACTATGTAGACCGGTTCTATAAAACTCTAAGAG
CCGAGCAAGCTTCACAGGAAGTAAAAAATTGGATGACAGAAACCTTGTTGGTCCAAAATG
CGAACCCAGATTGTAAGACTATTTTAAAAGCATTGGGACCAGCGGCTACACTAGAAGAAA
TGATGACAGCATGTCAGGGAGTAGGAGGACCCGGCCATAAGGCAAGAGTTTTGGCTGAAG
CAATGAGCCAAGTAACAAATTCAACTACCATAATGATGCAAAGAGGCAATTTTAGGAACC
AAAGAAAAATTGTTAAGTGTTTCAATTGTGGCAAAGAAGGGCACATAGCAAGAAATTGCA
AGGCCCCTAGAAAAAAGGGCTGTTGGAAATGTGGAAAGGAAGGACACCAAATGAAAGATT
GTACTGAGAGACAGGCTAATTTTTTAGGGAAGATCTGGCCTTCCTACAAGGGAAGGCCAG
GGAATTTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCATTTCTTCAGAGCAGACCAG
AGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTCTGGGGTAGAGACAACAACTCCCCCTC
AGAAGCAGGAGCCGATAGACAAGGAACTGTATCCTTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04587
UniProtKB Entry NamePOL_HV1B5
GenBank Protein ID327460
GenBank Gene IDK02012
PDB ID(s)1BDL, 1BDQ, 1BDR, 1FEJ, 1FF0, 1FFF, 1FFI, 1FG6, 1FG8, 1FGC, 1G2K, 1HPV, 1HVJ, 1HVS, 1K1T, 1K1U, 1K2B, 1K2C, 1ODX, 1Q9P, 1TCX, 1WJE, 1WJF, 2AOC, 2AOD, 2AOE, 2AOF, 2AOG, 2AOH, 2AOI, 2AOJ, 2AVM, 2AVO, 2AVQ, 2AVS, 2AVV, 2BPV, 2BPW, 2BPX, 2BPY, 2BPZ, 2F80, 2F81, 2F8G, 2G3L, 2NMY, 2NMZ, 2NNK, 2NNP, 2R38, 2R3T, 2R3W, 2Z54, 3B7V, 3B80, 3BC4, 3BGB, 3BGC, 3CYW, 3CYX, 3D1X, 3D1Y, 3D1Z, 3D20, 3OXC
General References
  1. Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K, et al.: Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature. 1985 Jan 24-30;313(6000):277-84. [Article]
  2. Vogt VM: Proteolytic processing and particle maturation. Curr Top Microbiol Immunol. 1996;214:95-131. [Article]
  3. Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32. [Article]
  4. Negroni M, Buc H: Mechanisms of retroviral recombination. Annu Rev Genet. 2001;35:275-302. [Article]
  5. Dunn BM, Goodenow MM, Gustchina A, Wlodawer A: Retroviral proteases. Genome Biol. 2002;3(4):REVIEWS3006. Epub 2002 Mar 26. [Article]
  6. Scarlata S, Carter C: Role of HIV-1 Gag domains in viral assembly. Biochim Biophys Acta. 2003 Jul 11;1614(1):62-72. [Article]
  7. Thaisrivongs S, Watenpaugh KD, Howe WJ, Tomich PK, Dolak LA, Chong KT, Tomich CC, Tomasselli AG, Turner SR, Strohbach JW, et al.: Structure-based design of novel HIV protease inhibitors: carboxamide-containing 4-hydroxycoumarins and 4-hydroxy-2-pyrones as potent nonpeptidic inhibitors. J Med Chem. 1995 Sep 1;38(18):3624-37. [Article]
  8. Hoog SS, Towler EM, Zhao B, Doyle ML, Debouck C, Abdel-Meguid SS: Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity. Biochemistry. 1996 Aug 13;35(32):10279-86. [Article]
  9. Towler EM, Thompson SK, Tomaszek T, Debouck C: Identification of a loop outside the active site cavity of the human immunodeficiency virus proteases which confers inhibitor specificity. Biochemistry. 1997 Apr 29;36(17):5128-33. [Article]
  10. Cai M, Zheng R, Caffrey M, Craigie R, Clore GM, Gronenborn AM: Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nat Struct Biol. 1997 Jul;4(7):567-77. [Article]
  11. Swairjo MA, Towler EM, Debouck C, Abdel-Meguid SS: Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease. Biochemistry. 1998 Aug 4;37(31):10928-36. [Article]
  12. Cai M, Huang Y, Caffrey M, Zheng R, Craigie R, Clore GM, Gronenborn AM: Solution structure of the His12 --> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium. Protein Sci. 1998 Dec;7(12):2669-74. [Article]
  13. Mahalingam B, Louis JM, Hung J, Harrison RW, Weber IT: Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes. Proteins. 2001 Jun 1;43(4):455-64. [Article]
  14. Schaal W, Karlsson A, Ahlsen G, Lindberg J, Andersson HO, Danielson UH, Classon B, Unge T, Samuelsson B, Hulten J, Hallberg A, Karlen A: Synthesis and comparative molecular field analysis (CoMFA) of symmetric and nonsymmetric cyclic sulfamide HIV-1 protease inhibitors. J Med Chem. 2001 Jan 18;44(2):155-69. [Article]
  15. Mahalingam B, Boross P, Wang YF, Louis JM, Fischer CC, Tozser J, Harrison RW, Weber IT: Combining mutations in HIV-1 protease to understand mechanisms of resistance. Proteins. 2002 Jul 1;48(1):107-16. [Article]
  16. Ishima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM: Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. J Biol Chem. 2003 Oct 31;278(44):43311-9. Epub 2003 Aug 21. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
(2S)-2-amino-3-phenylpropane-1,1-diolexperimentalunknowntargetDetails
2-aminoethyl naphthalen-1-ylacetateexperimentalunknowntargetDetails