A Sequence-Ready Physical Map of the Region Containing the Human Natural Killer Gene Complex on Chromosome 12p12.3–p13.2

Renedo, Mónica; Arce, Ignacio; Montgomery, Kate; Roda-Navarro, Pedro; Lee, Eunice; Kucherlapati, Raju; Fernández‐Ruiz, Elena

doi:10.1006/geno.2000.6163

Cited by 38 publications

(24 citation statements)

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“…LOX-1 exhibits the highest protein sequence similarity to the members of group-II C-type animal lectins including natural killer (NK) cell receptors [20,30,31]. Although the topology for LOX-1 was not determined, recent studies have identified the crystal structure of lectin-like NK cell receptors [32,33].…”

Section: Discussionmentioning

confidence: 99%

Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding

CHEN

NARUMIYA

Masaki

et al. 2001

Biochemical Journal

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Lectin-like oxidized low-density-lipoprotein (oxLDL) receptor-1 (LOX-1) is a cell-surface endocytosis receptor for atherogenic oxLDL, which is highly expressed in endothelial cells. Recent studies suggest that it may play significant roles in atherogenesis. LOX-1 is a type-II membrane protein that structurally belongs to the C-type lectin family molecules. This study was designed to characterize the specific domain on LOX-1 that recognizes oxLDL. Truncation of the lectin domain of LOX-1 abrogated oxLDL-binding activity. Deletion of the utmost C-terminal ten amino acid residues (261-270) was enough to disrupt the oxLDL-binding activity. Substitutions of Lys-262 and/or Lys-263 with Ala additively attenuated the activity. Serial-deletion analysis showed that residues up to 265 are required for the expression of minimal binding activity, although deletion of the C-terminal three residues (268-270) still retained full binding activity. Consistently, these alterations in LOX-1 impaired the recognition by a functionally blocking monoclonal antibody for LOX-1. These data demonstrated the distinct role of the lectin domain as the functional domain recognizing LOX-1 ligand. The conserved C-terminal residues of lectin-like domain are essential for binding oxLDL. Particularly, the basic amino acid pair is important for the binding.

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Section: Discussionmentioning

confidence: 99%

Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding

CHEN

NARUMIYA

Masaki

et al. 2001

Biochemical Journal

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“…The Lec2 gene encodes a C-type lectin-like protein deduced to consist of 156 aa with amino acid sequence similarities to the C-type lectin-like domains of a human lectin-like NK cell receptor protein LLT1 (43% identity), human AICL (40% identity), mouse CLRF (42% identity), and a human early lymphocyte activation Ag CD69 (34% identity) (GenBank accession numbers AF133299, X96719, AF350410, and Z30426, respectively). All of the human genes encoding these proteins are located within the NK cell receptor region on the chromosome 12p13-p12 (37).…”

Section: Coja-bg -Lec and -Nk Genesmentioning

confidence: 99%

Comparative Genomic Analysis of Two Avian (Quail and Chicken) MHC Regions

Shiina

Shimizu

Hosomichi

et al. 2004

The Journal of Immunology

147

127

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We mapped two different quail Mhc haplotypes and sequenced one of them (haplotype A) for comparative genomic analysis with a previously sequenced haplotype of the chicken Mhc. The quail haplotype A spans 180 kb of genomic sequence, encoding a total of 41 genes compared with only 19 genes within the 92-kb chicken Mhc. Except for two gene families (B30 and tRNA), both species have the same basic set of gene family members that were previously described in the chicken “minimal essential” Mhc. The two Mhc regions have a similar overall organization but differ markedly in that the quail has an expanded number of duplicated genes with 7 class I, 10 class IIB, 4 NK, 6 lectin, and 8 B-G genes. Comparisons between the quail and chicken Mhc class I and class II gene sequences by phylogenetic analysis showed that they were more closely related within species than between species, suggesting that the quail Mhc genes were duplicated after the separation of these two species from their common ancestor. The proteins encoded by the NK and class I genes are known to interact as ligands and receptors, but unlike in the quail and the chicken, the genes encoding these proteins in mammals are found on different chromosomes. The finding of NK-like genes in the quail Mhc strongly suggests an evolutionary connection between the NK C-type lectin-like superfamily and the Mhc, providing support for future studies on the NK, lectin, class I, and class II interaction in birds.

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“…NKG2-A, -C, -E and NKG2-F share substantial sequence homology, while NKG2-D is distantly related to the other NKG2 family members. [20][21][22] In contrast to killer cell Ig-like receptor (KIR) genes, where the number of loci possessed by an individual is variable because of the structural polymorphism of the leukocyte receptor complex (LRC) on chromosome 19q13, gross structural polymorphism of the NKG2 gene family has not been known, and all individuals are assumed to possess all of the NKG2 genes. 23,24 Although recent reports demonstrated polymorphisms of NKG2 and CD94 genes from the analysis of a relatively small number of healthy individuals, 23,25 neither population-based variation screening, nor analysis on the association between the polymorphisms and rheumatic diseases, has been reported.…”

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confidence: 99%

Variations of human killer cell lectin-like receptors: common occurrence of NKG2-C deletion in the general population

et al. 2003

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CD94 and NKG2 are members of the NK cell receptor families, and are encoded in the natural killer gene complex (NKC) on human chromosome 12p12-13, one of the candidate chromosomal regions for rheumatic diseases. To examine a possible association between variations in CD94 and NKG2 genes and genetic susceptibility to rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE), we carried out a systematic polymorphism screening of NKG2-A (KLRC1), NKG2-C (KLRC2) and CD94 (KLRD1) genes on a population basis. In NKG2-A, previously considered to be highly conserved, 10 polymorphisms in the noncoding region and introns, as well as one rare variation leading to an amino acid substitution within the transmembrane region, c.238T4A (Cys80Ser), were detected. In NKG2-C, in addition to the previously described two nonsynonymous substitutions, c.5G4A (Ser2Asn) and c.305C4T (Ser102Phe), two polymorphisms were newly detected in the noncoding region. In CD94, only one single nucleotide substitution was identified in the 5 0 untranslated region. When the patients and healthy individuals were genotyped for these variations, no significant association was observed. However, although statistically not significant, NKG2-A c.238T4A (Cys80Ser) was observed in three patients with RA, but in none of the healthy individuals and the patients with SLE. Unexpectedly, in the process of polymorphism screening, we identified homozygous deletion of NKG2-C in approximately 4.3% of healthy donors; under the assumption of Hardy-Weinberg equilibrium, the allele frequency of NKG2-C deletion was estimated to be 20.7%. These results demonstrated that, although human NKG2-A, -C and CD94 are generally conserved with respect to amino acid sequences, NKG2-A is polymorphic in the noncoding region, and that the number of genes encoded in the human NKC is variable among individuals, as previously shown for the leukocyte receptor complex (LRC), HLA and Fcg receptor (FCGR) regions.

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A Sequence-Ready Physical Map of the Region Containing the Human Natural Killer Gene Complex on Chromosome 12p12.3–p13.2

Cited by 38 publications

References 50 publications

Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding

Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding

Comparative Genomic Analysis of Two Avian (Quail and Chicken) MHC Regions

Variations of human killer cell lectin-like receptors: common occurrence of NKG2-C deletion in the general population

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