Heliks-zavoj-heliks

HTH DNA vezujući domen
HTH DNA vezujući domen
Identifikatori
Simbol	HTH_10
Pfam	PF04967
Pfam klan	CL0123
InterPro	IPR007050
Pfam
Dostupne proteinske strukture:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Dostupne proteinske strukture:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Bakterijski regulatorni heliks-zavoj-heliks protein, lysR familija
Bakterijski regulatorni heliks-zavoj-heliks protein, lysR familija
Identifikatori
Simbol	HTH_1
Pfam	PF00126
Pfam klan	CL0123
InterPro	IPR000847
PROSITE	PDOC00043
SCOP	1al3
SUPERFAMILY	1al3
Pfam
Dostupne proteinske strukture:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

U proteinima, heliks-zavoj-heliks (HTH) je glavni strukturni motiv sa sposobnošću vezivanja za DNK. On se sastoji od dva α heliksa spojena kratkim lancom aminokiselina. Prisutan je u mnogim proteinima koji regulišu ekspresiju gena. On se razlikuje od domena heliks-petlja-heliks.^[1]

Otkriće

Otkriće heliks-zavoj-heliks motiva je bilo bazirano na sličnostima između nekoliko gena koji koriraju transkripcione regulatorne proteine iz bakteriofaga lambda i Escherichia coli: Cro, CAP, i λ represor, za koje je najđeno da imaju zajedničku 20-25 aminokiselina dugu sekvencu koja omogućava DNK prepoznavanje.^[2]^[3]^[4]^[5]

^ Brennan RG, Matthews BW (1989). „The helix-turn-helix DNA binding motif.”. J Biol Chem. 264 (4): 1903—6. PMID 2644244.
^ Matthews BW, Ohlendorf DH, Anderson WF, Takeda Y (1982). „Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor.”. Proc Natl Acad Sci U S A. 79 (5): 1428—32. PMC 345986 . PMID 6951187.
^ Anderson WF, Ohlendorf DH, Takeda Y, Matthews BW (1981). „Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.”. Nature. 290 (5809): 754—8. PMID 6452580.
^ McKay DB, Steitz TA (1981). „Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.”. Nature. 290 (5809): 744—9. PMID 6261152.
^ Pabo CO, Lewis M (1982). „The operator-binding domain of lambda repressor: structure and DNA recognition.”. Nature. 298 (5873): 443—7. PMID 7088190.

K, Struhl (1989). „Helix-turn-helix, zinc-finger, and leucine-zipper motifs for eukaryotic transcriptional regulatory proteins.”. Trends Biochem Sci. 14 (4): 137—40. PMID 2499084.
Gajiwala KS, Burley SK (2000). „Winged helix proteins.”. Curr Opin Struct Biol. 10 (1): 110—6. PMID 10679470.
Santos CL, Tavares F, Thioulouse J, Normand P (2009). „A phylogenomic analysis of bacterial helix-turn-helix transcription factors.”. FEMS Microbiol Rev. 33 (2): 411—29. PMID 19076237. doi:10.1111/j.1574-6976.2008.00154.x.
Hoskisson PA, Rigali S (2009). „Chapter 1: Variation in form and function the helix-turn-helix regulators of the GntR superfamily.”. Adv Appl Microbiol. 69: 1—22. PMID 19729089. doi:10.1016/S0065-2164(09)69001-8.
RG, Brennan (1993). „The winged-helix DNA-binding motif: another helix-turn-helix takeoff.”. Cell. 74 (5): 773—6. PMID 8374950.
Huffman JL, Brennan RG (2002). „Prokaryotic transcription regulators: more than just the helix-turn-helix motif.”. Curr Opin Struct Biol. 12 (1): 98—106. PMID 11839496.

Heliks-zavoj-heliks domeni

Ribonukleazni R heliksni domen

Identifikatori

Simbol

HTH_12