

RT- Reverse Transcriptase
HIV RT forms a heterodimer with RT/RNase H
polyprotein and reverse transcribes viral RNA into DNA.
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[animated
gif: 320x240 ]
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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]
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Reference
Sequences:
HIV-1
(HXB2):
10 20 30 40 50 60 70 | | | | | | | PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV FAIKKKDSTK 80 90 100 110 120 130 140 | | | | | | | WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL DEDFRKYTAF TIPSINNETP 150 160 170 180 190 200 210 | | | | | | | GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPDIVI YQYMDDLYVG SDLEIGQHRT KIEELRQHLL 220 230 240 250 260 270 280 | | | | | | | RWGLTTPDKK HQKEPPFLWM GYELHPDKWT VQPIVLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVRQLC 290 300 310 320 330 340 350 | | | | | | | KLLRGTKALT EVIPLTEEAE LELAENREIL KEPVHGVYYD PSKDLIAEIQ KQGQGQWTYQ IYQEPFKNLK 360 370 380 390 400 410 420 | | | | | | | TGKYARMRGA HTNDVKQLTE AVQKITTESI VIWGKTPKFK LPIQKETWET WWTEYWQATW IPEWEFVNTP 430 440 | | 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]
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Identifiers:
ViralZone:
HIV-1
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]
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- 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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