Leucine-rich repeat

Leucine-rich repeat

Symbol = LRR_1
Name =

width =
caption = An example of a leucine-rich repeat protein, a porcine ribonuclease inhibitor
Pfam= PF00560
InterPro= IPR001611
Prosite =
SCOP = 1bnh
OPM family=
OPM protein= 1xwd
PDB=PDB3|1ogqA:155-177 PDB3|1jl5A:358-382 PDB3|1g9uA:358-382PDB3|1k5dF:123-149 PDB3|2ca6A:123-149 PDB3|1yrgA:123-149PDB3|1k5gF:123-149 PDB3|1k15A:165-187 PDB3|1m0zA:165-187PDB3|1u0nD:165-187 PDB3|1qyyG:165-187 PDB3|1sq0B:165-187PDB3|1m10B:165-187 PDB3|1ookG:165-187 PDB3|1k13A:165-187PDB3|1p9aG:165-187 PDB3|1p8vA:165-187 PDB3|1k14A:165-187PDB3|1ziwA:563-585 PDB3|2a0zA:563-585 PDB3|1wwlA:292-318PDB3|1p8tA:131-153 PDB3|1oznA:131-153 PDB3|1xum :54-75PDB3|1xcdA:131-149 PDB3|1xecB:131-149 PDB3|1xkuA:131-149PDB3|1xwdC:194-217 PDB3|1xun :194-217 PDB3|1o6sA:274-294PDB3|1kohB:292-315 PDB3|1fo1B:292-315 PDB3|1ft8D:292-315PDB3|1kooC:292-315 PDB3|2bnh :337-360 PDB3|1dfjI:337-360PDB3|1a4yD:114-137 PDB3|2bexA:114-137 PDB3|1z7xW:114-137PDB3|1dceA:509-532 PDB3|1ltxA:509-532 PDB3|1p95B:551-560PDB3|1xeuA:162-182 PDB3|1m9lA:116-139 PDB3|1ds9A:116-139PDB3|1m9sA:165-185 PDB3|1h6tA:165-185 PDB3|1otmA:165-185PDB3|1otoA:165-185 PDB3|1d0bA:165-185 PDB3|1otnA:165-185PDB3|1h6uA:209-229 PDB3|1w8aA:596-618 PDB3|1a9nA:89-109

A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20-30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tighly sterically packed with leucine residues.


Leucine-rich repeat motifs have been identified in a large number of functionally unrelated proteins. The best-known example is the ribonuclease inhibitor, but other proteins such as the tropomyosin regulator tropomodulin and the toll-like receptor also share the motif. In fact, the toll-like receptor possesses 10 successive LRR motifs which serve to bind antigen.

Although the canonical LRR protein contains approximately one helix for every beta strand, variants that form beta-alpha superhelix folds sometimes have long loops rather than helices linking successive beta strands.

ee also

*Leucine zipper

External links

* [http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.bb.html SCOP LRR fold]
* [http://www.cathdb.info/cgi-bin/cath/GotoCath.pl?cath=3.80 CATH Alpha-beta horseshoe architecture]


* Branden C, Tooze J. (1999). "Introduction to Protein Structure" 2nd ed. Garland Publishing: New York, NY.

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