RT- Reverse Transcriptase
HIV
RT forms a heterodimer with RT/RNase H polyprotein and
reverse transcribes viral RNA into DNA.
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Isoforms:
- p51 (440 amino acids) - Reverse Transcriptase
- p66 (560 amino acids) - RT + RNase H
Cleavage
site:
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Localization:
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Function:
- RT makes a double-stranded DNA copy of the dimer of
single-stranded RNA
- RT has both RNA-dependant and DNA-dependant polymerase
activity
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Additional
Information:
- RT has low fidelity (high frequency of mutation)
- viral DNA can be completely synthesized within 6 hours of viral
entry
- major functional species of polymerase is a heterodimer of p50
(Reverse Transcriptase) and p65 (Reverse Transcriptase - RNase H) (Ref.
#4)
- many cis-acting elements in viral RNA are required for the
generation of viral DNA (Ref. #5)
- TAR is a small RNA stem-loop structure located at 5'-end of
viral RNA and is required for initiation of Reverse Transcriptase (Ref.
#5)
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Genomic Location: [TOP] |
Reference
Sequences:
HIV-1
(HXB2): 10 20 30 40 50 60 70
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PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV FAIKKKDSTK
80 90 100 110 120 130 140
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WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL DEDFRKYTAF TIPSINNETP
150 160 170 180 190 200 210
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GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPDIVI YQYMDDLYVG SDLEIGQHRT KIEELRQHLL
220 230 240 250 260 270 280
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RWGLTTPDKK HQKEPPFLWM GYELHPDKWT VQPIVLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVRQLC
290 300 310 320 330 340 350
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KLLRGTKALT EVIPLTEEAE LELAENREIL KEPVHGVYYD PSKDLIAEIQ KQGQGQWTYQ IYQEPFKNLK
360 370 380 390 400 410 420
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TGKYARMRGA HTNDVKQLTE AVQKITTESI VIWGKTPKFK LPIQKETWET WWTEYWQATW IPEWEFVNTP
430 440
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PLVKLWYQLE KEPIVGAETF
[download in fasta format]
Length:
440 amino acids (residues 155 to 585)
Molecular Weight: 51330
Da
Theoretical pI: 8.64
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Protein Domains/Folds/Motifs: [TOP]
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InterPro
signature for RNA-directed DNA polymerase - IPR000477
InterPro
signature for Reverse Transcriptase connection domain - IPR010659
InterPro
signature for Reverse Transcriptase thumb domain - IPR010661
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Secondary Structure predictions:
Low Complexity Regions - seg:
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N-glycosylation:
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N-myristoylation:
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Amidation:
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Protein kinase C:
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Casein kinase II:
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Tyrosine kinase:
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cAMP / cGMP kinase:
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Cell attachment motif:
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Asp Protease motif:
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Asp Prot Retro motif:
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Cysteine-rich Region:
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Tryptophan-rich Region:
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Zinc-finger CCHC motif:
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Leucine Zipper motif:
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Protein-Protein Interactions: [TOP]
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Primary and Secondary Database Entries:
[TOP] |
Identifiers:
PDB/MMDB: Search for HIV-1 & RT
SwissProt:
P04585
(HIV-1 HXB2 POL)
EC: 2.7.7.49
EMBL:
K03455; AAB50259.1 [EMBL/GenBank/DDBJ]
PIR:
UNKNOWN
HIV: K03455; UNKNOWN$HXB2
InterPro: IPR008187UNKNOWN
Pfam:
PF00558UNKNOWN
Prints:
none
ProDom:
PD000261 (1 - 62) /
PD580497 (29 - 72) /
PD492067 (63 - 105) /
PD404869 (63 - 130)
PD000379 (106 - 148) /
PD693134 (119 - 168) /
PD513590 (121 - 161) /
PD474846 (139 - 234)
PD000698 (235 - 296) /
PD495523 (307 - 438)
SCOP: SSF56672 DNA/RNA polymerase
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
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Reviews and References: [TOP] |
- 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
- Crystal structure at 3.5 A resolution of HIV-1 reverse
transcriptase complexed with an inhibitor.
- Kohlstaedt
LA, Wang J, Friedman JM.
- Science
256: 1783-1790 (1992) [pubmed: 1377403]
- 5
- A critical role for the TAR element in promoting efficient human
immunodeficiency virus type 1
- reverse
transcription.
- Harrich
D, Ulich C, Gaynor RB.
- J
Virol 70: 4017-4127 (1996) [pubmed: 8648739]
- 6 - [HIV RT Review] Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase:
- implications for drug resistance.
- Huang H, Chopra R, Verdine GL, Harrison SC.
- Science 282(5394): 1669-1675 (1998) [pubmed: 9831551]
- 7 - [Website] An accurate look into HIV
- Teresa Larsen
- The Scripp Research Institute - Website: http://www.sdsc.edu/GatherScatter/GSsummer96/larsen.html
- 8 - [Website] HIV-1 RT
- Kaylan Das
- Rutgers University - Website: http://www.cabm.rutgers.edu/~kalyan/RT_imgs/index.html
- 9 - [Website] HIV Drug Resistance Database
- Stanford
- Website: http://hivdb.stanford.edu
- 10 - [Website] HIV Drug Resistance Database
- Los Alamos National Labs
- Website: http://resdb.lanl.gov/Resist_DB/default.htm
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