Protein Domain : IPR003590

Type:  Repeat Name:  Leucine-rich repeat, ribonuclease inhibitor subtype
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 []. The 3-D structure of ribonuclease inhibitor, a protein containing 15 LRRs, has been determined [], revealing LRRs to be a new class of alpha/beta fold. LRRs form elongated non-globular structures and are often flanked by cysteine rich domains. This subtype is found in ribonuclease inhibitors. Short Name:  Leu-rich_rpt_RNase_inh_sub-typ

0 Child Features

0 Contains

1 Cross References

Identifier
SM00368

0 Found In

0 GO Annotation

0 Parent Features

1185 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
114118 D8SCE4 PAC:15416826 Selaginella moellendorffii 507  
447514 D8T029 PAC:15403712 Selaginella moellendorffii 655  
31008 D8RVA7 PAC:15413915 Selaginella moellendorffii 521  
405633 D8QZ75 PAC:15414716 Selaginella moellendorffii 572  
440378 D8RBD5 PAC:15404153 Selaginella moellendorffii 598  
410934 D8RGC0 PAC:15409491 Selaginella moellendorffii 445  
425099 PAC:15402243 Selaginella moellendorffii 1375  
93050 D8RF61 PAC:15418310 Selaginella moellendorffii 475  
418913 D8S777 PAC:15410548 Selaginella moellendorffii 1164  
442643 D8RV08 PAC:15412358 Selaginella moellendorffii 1293  
evm.model.supercontig_1278.2 PAC:16407429 Carica papaya 539  
evm.model.supercontig_370.5 PAC:16418782 Carica papaya 485  
evm.model.supercontig_42.108 PAC:16419688 Carica papaya 710  
evm.model.supercontig_46.67 PAC:16420535 Carica papaya 578  
evm.model.supercontig_60.94 PAC:16423789 Carica papaya 407  
evm.model.supercontig_8.207 PAC:16426494 Carica papaya 280  
27613.m000634 B9SSS4 PAC:16798808 Ricinus communis 1384  
29647.m002085 B9S424 PAC:16804729 Ricinus communis 546  
29736.m002117 B9S2J9 PAC:16807222 Ricinus communis 607  
29844.m003357 B9RTY6 PAC:16811064 Ricinus communis 549  
30136.m001005 B9RTZ8 PAC:16819134 Ricinus communis 1327  
30204.m001821 B9S586 PAC:16823938 Ricinus communis 598  
Cucsa.388720.1 A0A0A0K764 PAC:16982890 Cucumis sativus 539  
Cucsa.033700.1 PAC:16952559 Cucumis sativus 222  
Cucsa.033720.1 PAC:16952561 Cucumis sativus 278  
Cucsa.078730.1 PAC:16956125 Cucumis sativus 441  
Cucsa.101100.1 PAC:16958645 Cucumis sativus 1348  
Cucsa.254150.1 A0A0A0L502 PAC:16972205 Cucumis sativus 540  
GSVIVT01020179001 PAC:17829646 Vitis vinifera 630  
GSVIVT01014452001 PAC:17825434 Vitis vinifera 401  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1657640
            2176636
            11751054
            11967365
            14747988
            8264799