User:JonSDSUGrad/Sandbox/TEST11 HLA-B

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Major histocompatibility complex, class I, B, also known as HLA-B, is a human gene.

Major histocompatibility complex, class I, B
PDB rendering based on 1a1n.
Available structures: 1a1n, 1a9b, 1a9e, 1agb, 1agc, 1agd, 1age, 1agf, 1cg9, 1e27, 1e28, 1efx, 1hsa, 1jgd, 1jge, 1k5n, 1m05, 1mi5, 1of2, 1ogt, 1uxs, 1uxw, 1w0v, 1w0w, 1xh3, 1xr8, 1xr9, 1zhk, 1zhl, 1zsd, 2a83, 2ak4, 2axf, 2axg, 2bsr, 2bss, 2bst, 2cik, 2fyy, 2fz3, 2h6p, 2nw3, 2nx5
Identifiers
Symbol(s) HLA-B; HLA B; SPDA1
External IDs OMIM: 142830 HomoloGene: 83181
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3106 547349
Ensembl ENSG00000204523 n/a
Uniprot P01889 n/a
Refseq NM_005514 (mRNA)
NP_005505 (protein)		 NM_001025208 (mRNA)
NP_001020379 (protein)
Location Chr 6: 31.43 - 31.43 Mb n/a
Pubmed search [1] [2]

HLA-B belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exon 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-B alleles have been described[1]

[edit] References

  1. ^ Entrez Gene: HLA-B major histocompatibility complex, class I, B.

[edit] Further reading

  • Parham P, Benjamin RJ, Chen BP, et al. (1990). "Diversity of class I HLA molecules: functional and evolutionary interactions with T cells.". Cold Spring Harb. Symp. Quant. Biol. 54 Pt 1: 529-43. PMID 2700944. 
  • Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580-5. doi:10.1093/embo-reports/kve141. PMID 11463741. 
  • Greenway AL, Holloway G, McPhee DA, et al. (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323-35. PMID 12734410. 
  • Bénichou S, Benmerah A (2003). "[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway]". Med Sci (Paris) 19 (1): 100-6. PMID 12836198. 
  • Piancatelli D, Canossi A, Aureli A, et al. (2004). "Human leukocyte antigen-A, -B, and -Cw polymorphism in a Berber population from North Morocco using sequence-based typing.". Tissue Antigens 63 (2): 158-72. PMID 14705987. 
  • Leavitt SA, SchOn A, Klein JC, et al. (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm.". Curr. Protein Pept. Sci. 5 (1): 1-8. PMID 14965316. 
  • Arayssi T, Hamdan A (2004). "New insights into the pathogenesis and therapy of Behçet's disease.". Current opinion in pharmacology 4 (2): 183-8. doi:10.1016/j.coph.2003.10.009. PMID 15063364. 
  • Tolstrup M, Ostergaard L, Laursen AL, et al. (2004). "HIV/SIV escape from immune surveillance: focus on Nef.". Curr. HIV Res. 2 (2): 141-51. PMID 15078178. 
  • Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87-94. PMID 15638726. 
  • Anderson JL, Hope TJ (2005). "HIV accessory proteins and surviving the host cell.". Current HIV/AIDS reports 1 (1): 47-53. PMID 16091223. 
  • Grubić Z (2007). "[Hla-B27 gene: polymorphism, evolution, distribution, and association with spondyloartopathies]". Reumatizam 53 (1): 5-10. PMID 17580542.