NHL repeat

NHL repeat

Structure of the brain tumor-Pumilio translation repressor complex.[1]
Identifiers
Symbol NHL
Pfam PF01436
Pfam clan CL0186
InterPro IPR001258
SCOP 1q7f
SUPERFAMILY 1q7f

The NHL repeat, named after NCL-1, HT2A and Lin-41, is an amino acid sequence found largely in a large number of eukaryotic and prokaryotic proteins. For example, the repeat is found in a variety of enzymes of the copper type II, ascorbate-dependent monooxygenase family which catalyse the C-terminus alpha-amidation of biological peptides.[2] In many it occurs in tandem arrays, for example in the RING finger beta-box, coiled-coil (RBCC) eukaryotic growth regulators.[3] The 'Brain Tumor' protein (Brat) is one such growth regulator that contains a 6-bladed NHL-repeat beta-propeller.[1][4]

The NHL repeats are also found in serine/threonine protein kinase (STPK) in diverse range of pathogenic bacteria. These STPK are transmembrane receptors with an intracellular N-terminal kinase domain and extracellular C-terminal sensor domain. In the STPK, PknD, from Mycobacterium tuberculosis, the sensor domain forms a rigid, six-bladed b-propeller composed of NHL repeats with a flexible tether to the transmembrane domain.

References

  1. 1 2 Edwards TA, Wilkinson BD, Wharton RP, Aggarwal AK (October 2003). "Model of the brain tumor-Pumilio translation repressor complex". Genes Dev. 17 (20): 2508–2513. doi:10.1101/gad.1119403. PMC 218144Freely accessible. PMID 14561773.
  2. Kano S, Miyajima N, Fukuda S, Hatakeyama S (July 2008). "Tripartite motif protein 32 facilitates cell growth and migration via degradation of Abl-interactor 2". Cancer Res. 68 (14): 5572–5580. doi:10.1158/0008-5472.CAN-07-6231. PMID 18632609.
  3. Slack FJ, Ruvkun G (December 1998). "A novel repeat domain that is often associated with RING finger and B-box motifs". Trends Biochem. Sci. 23 (12): 474–5. doi:10.1016/S0968-0004(98)01299-7. PMID 9868369.
  4. Edwards TA, Pyle SE, Wharton RP, Aggarwal AK (April 2001). "Structure of Pumilio reveals similarity between RNA and peptide binding motifs". Cell. 105 (2): 281–9. doi:10.1016/S0092-8674(01)00318-X. PMID 11336677.

This article incorporates text from the public domain Pfam and InterPro IPR001258

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