 Helix-Turn-Helix Motifs
"Helix-Turn-Helix Motifs" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The first DNA-binding protein motif to be recognized. Helix-turn-helix motifs were originally identified in bacterial proteins but have since been found in hundreds of DNA-BINDING PROTEINS from both eukaryotes and prokaryotes. They are constructed from two alpha helices connected by a short extended chain of amino acids, which constitute the "turn." The two helices are held at a fixed angle, primarily through interactions between the two helices. (From Alberts et al., Molecular Biology of the Cell, 3d ed, p408-9)
| Descriptor ID |
D019077
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| MeSH Number(s) |
G02.111.570.820.709.275.500.360.360
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| Concept/Terms |
Helix-Turn-Helix Motifs- Helix-Turn-Helix Motifs
- Helix Turn Helix Motifs
- Helix-Turn-Helix Motif
- Motif, Helix-Turn-Helix
- Motifs, Helix-Turn-Helix
- Motifs, Helix Turn Helix
- HTH Motifs
- HTH Motif
- Motif, HTH
- Motifs, HTH
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Below are MeSH descriptors whose meaning is more general than "Helix-Turn-Helix Motifs".
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This graph shows the total number of publications written about "Helix-Turn-Helix Motifs" by people in this website by year, and whether "Helix-Turn-Helix Motifs" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
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| 2004 | 0 | 1 | 1 | | 2006 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 |
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Below are the most recent publications written about "Helix-Turn-Helix Motifs" by people in Profiles.
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Klocko AD, Wassarman KM. 6S RNA binding to Esigma(70) requires a positively charged surface of sigma(70) region 4.2. Mol Microbiol. 2009 Jul; 73(2):152-64.
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Liu Y, Manna AC, Pan CH, Kriksunov IA, Thiel DJ, Cheung AL, Zhang G. Structural and function analyses of the global regulatory protein SarA from Staphylococcus aureus. Proc Natl Acad Sci U S A. 2006 Feb 14; 103(7):2392-7.
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Lindhout DA, Litowski JR, Mercier P, Hodges RS, Sykes BD. NMR solution structure of a highly stable de novo heterodimeric coiled-coil. Biopolymers. 2004 Dec 05; 75(5):367-75.
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Breitinger HG, Lanig H, Vohwinkel C, Grewer C, Breitinger U, Clark T, Becker CM. Molecular dynamics simulation links conformation of a pore-flanking region to hyperekplexia-related dysfunction of the inhibitory glycine receptor. Chem Biol. 2004 Oct; 11(10):1339-50.
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Litowski JR, Hodges RS. Designing heterodimeric two-stranded alpha-helical coiled-coils. Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity. J Biol Chem. 2002 Oct 04; 277(40):37272-9.
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Kohn WD, Mant CT, Hodges RS. Alpha-helical protein assembly motifs. J Biol Chem. 1997 Jan 31; 272(5):2583-6.
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