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
- Functionsaspartic-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 bindingProcessesDNA 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 cellComponentshost 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
Resource Link UniProtKB ID P04587 UniProtKB Entry Name POL_HV1B5 GenBank Protein ID 327460 GenBank Gene ID K02012 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
- 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]
- Vogt VM: Proteolytic processing and particle maturation. Curr Top Microbiol Immunol. 1996;214:95-131. [Article]
- Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32. [Article]
- Negroni M, Buc H: Mechanisms of retroviral recombination. Annu Rev Genet. 2001;35:275-302. [Article]
- Dunn BM, Goodenow MM, Gustchina A, Wlodawer A: Retroviral proteases. Genome Biol. 2002;3(4):REVIEWS3006. Epub 2002 Mar 26. [Article]
- Scarlata S, Carter C: Role of HIV-1 Gag domains in viral assembly. Biochim Biophys Acta. 2003 Jul 11;1614(1):62-72. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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
Drug Drug group Pharmacological action? Type Actions Details (2S)-2-amino-3-phenylpropane-1,1-diol experimental unknown target Details 2-aminoethyl naphthalen-1-ylacetate experimental unknown target Details