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Protein Domain : IPR000372

Name  Leucine-rich repeat-containing N-terminal Short Name  LRR-contain_N
Type  Domain Description  Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the beta-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear" segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with alpha-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain and a C-terminal LRR domain (). This entry represents the N-terminal LRR domain.

Publication Counts Displayer

0 Child Features

0 Contains

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PF01462 PFAM IPR000372
SM00013 SMART IPR000372

2 Data Sets

Name URL
Swiss-Prot data set http://ca.expasy.org/sprot
InterPro data set  

5 Found In

DB identifier Name Short Name Type
IPR020777 Tyrosine-protein kinase, neurotrophic receptor Tyr_kinase_NGF_rcpt Family
IPR020446 Tyrosine-protein kinase, neurotrophic receptor, type 3 Tyr_kin_neurotrophic_rcpt_3 Family
IPR020455 Tyrosine-protein kinase, neurotrophic receptor, type 2 Tyr_kin_neurotrophic_rcpt_2 Family
IPR000434 Polycystic kidney disease type 1 protein PKD_1 Family
IPR016352 Small leucine-rich proteoglycan, class I, decorin/asporin/byglycan SLRP_I_decor/aspor/byglycan Family

0 GO Annotation

0 Ontology Annotations

0 Parent Features

147 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0079369 Q9VLE6 Drosophila melanogaster
FBpp0085620 A1ZBR2 Drosophila melanogaster
FBpp0081104 Q9VIA4 Drosophila melanogaster
FBpp0297617 Q9VR83 Drosophila melanogaster
FBpp0085182 Q9V9V6 Drosophila melanogaster
FBpp0085638 Q7KIN0 Drosophila melanogaster
FBpp0084431 P08953 Drosophila melanogaster
FBpp0075624 Q9VU51 Drosophila melanogaster
FBpp0075570 Q9VU53 Drosophila melanogaster
FBpp0072828 Q9VZZ4 Drosophila melanogaster
FBpp0080311 Q9V430 Drosophila melanogaster
FBpp0075367 Q9VUN0 Drosophila melanogaster
FBpp0075360 Q9V477 Drosophila melanogaster
FBpp0080080 Q9VJX9 Drosophila melanogaster
FBpp0303575 P24014 Drosophila melanogaster
FBpp0303108 M9PFH7 Drosophila melanogaster
FBpp0291294 A1ZAB1 Drosophila melanogaster
FBpp0292107 Q9VU13 Drosophila melanogaster
FBpp0293933 Q0E8F0 Drosophila melanogaster
FBpp0298807 Q297R4 Drosophila pseudoobscura
FBpp0278316 Q28YE4 Drosophila pseudoobscura
FBpp0274771 Q2M1B0 Drosophila pseudoobscura
FBpp0285716 B5DK64 Drosophila pseudoobscura
FBpp0279399 B5DHL3 Drosophila pseudoobscura
FBpp0272993 Q29GW9 Drosophila pseudoobscura
FBpp0274067 Q2LYW7 Drosophila pseudoobscura
FBpp0274776 Q2M1B4 Drosophila pseudoobscura
FBpp0275146 Q2M032 Drosophila pseudoobscura
FBpp0275149 B5DPJ7 Drosophila pseudoobscura
FBpp0276540 B5E152 Drosophila pseudoobscura