PROSITE documentation PDOC51125
NHL repeat profile


The NHL repeat was defined by amino acid sequence homologies among Ncl-1, HT2A and Lin-41 proteins [1]. NHL is a conserved structural motif present in a large family of growth regulator. Many NHL containing proteins have additional domains such as a RING finger (see <PDOC00449>), a B-box zinc finger (see <PDOC50119>) or a coiled-coil motif. According to structural model analysis the NHL domain could be involved in protein-protein interaction [2].

The NHL domain is a six-bladed β-propeller, with the blades arrayed in a radial fashion around a central axis, and each blade composed of a highly twisted four stranded antiparallel β-sheet (see <PDB:1Q7F>) [2]. The innermost strand of each blade is labeled 'a' and the outermost strand, 'd'. Like in other β-propellers the sequence repeats are offset with respect to the blades of the propeller, such that any given 40-residue NHL repeat spans strands 'b-d' of one propeller blade and strand 'a' of the subsequent blade. This offset ensures circularization of the propeller because the last strand of the final sequence repeat acts as an innermost strand a of the blade that harbors strands 'b-d' from the first sequence repeat.

The profile we developed covers the whole NHL sequence repeat.

Last update:

June 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

NHL, PS51125; NHL repeat profile  (MATRIX)


1AuthorsSlack F.J. Ruvkun G.
TitleA novel repeat domain that is often associated with RING finger and B-box motifs.
SourceTrends Biochem. Sci. 23:474-475(1998).
PubMed ID9868369

2AuthorsEdwards T.A. Wilkinson B.D. Wharton R.P. Aggarwal A.K.
TitleModel of the brain tumor-Pumilio translation repressor complex.
SourceGenes Dev. 17:2508-2513(2003).
PubMed ID14561773

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