HLA-DMA

From Wikipedia, the free encyclopedia

Major histocompatibility complex, class II, DM alpha

PDB rendering based on 1hdm.

Available structures: 1hdm, 2bc4

Identifiers

Symbol(s)

HLA-DMA; D6S222E; DMA; HLADM; RING6

External IDs

OMIM: 142855 MGI: 95921 HomoloGene: 4464

Gene ontology
Molecular Function:	• protein binding • MHC class II receptor activity
Cellular Component:	• cellular_component • intracellular • lysosomal membrane • multivesicular body • endosome membrane • membrane • integral to membrane • MHC class II protein complex
Biological Process:	• antigen processing and presentation of peptide or polysaccharide antigen via MHC class II • protein complex assembly • immune response • biological_process • protein transport • immunoglobulin mediated immune response • antigen processing and presentation of exogenous peptide antigen via MHC class II • positive thymic T cell selection • positive regulation of T cell differentiation • positive regulation of immune response • chaperone cofactor-dependent protein folding

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006120 (mRNA)
NP_006111 (protein)

NM_010386 (mRNA)
NP_034516 (protein)

Location

Chr 6: 33.02 - 33.03 Mb

Chr 17: 33.75 - 33.75 Mb

Pubmed search

[1]

[2]

Major histocompatibility complex, class II, DM alpha, also known as HLA-DMA, is a human gene.^[1]

HLA-DMA belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DMA) and a beta chain (DMB), both anchored in the membrane. It is located in intracellular vesicles. DM plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa and its gene contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail.^[1]

[edit] References

^ ^a ^b Entrez Gene: HLA-DMA major histocompatibility complex, class II, DM alpha.

[edit] Further reading

Vogt AB, Kropshofer H (1999). "HLA-DM - an endosomal and lysosomal chaperone for the immune system.". Trends Biochem. Sci. 24 (4): 150–4. PMID 10322421.
Kropshofer H, Hämmerling GJ, Vogt AB (2000). "The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules.". Immunol. Rev. 172: 267–78. PMID 10631952.
Piatier-Tonneau D, Gastinel LN, Amblard F, et al. (1991). "Interaction of CD4 with HLA class II antigens and HIV gp120.". Immunogenetics 34 (2): 121–8. PMID 1869305.
Kelly AP, Monaco JJ, Cho SG, Trowsdale J (1991). "A new human HLA class II-related locus, DM.". Nature 353 (6344): 571–3. doi:10.1038/353571a0. PMID 1922365.
Kelly A, Powis SH, Glynne R, et al. (1991). "Second proteasome-related gene in the human MHC class II region.". Nature 353 (6345): 667–8. doi:10.1038/353667a0. PMID 1922385.
Rosenstein Y, Burakoff SJ, Herrmann SH (1990). "HIV-gp120 can block CD4-class II MHC-mediated adhesion.". J. Immunol. 144 (2): 526–31. PMID 1967269.
Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ (1991). "Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules.". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 9052–6. PMID 1978941.
Clayton LK, Sieh M, Pious DA, Reinherz EL (1989). "Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding.". Nature 339 (6225): 548–51. doi:10.1038/339548a0. PMID 2543930.
Diamond DC, Sleckman BP, Gregory T, et al. (1988). "Inhibition of CD4+ T cell function by the HIV envelope protein, gp120.". J. Immunol. 141 (11): 3715–7. PMID 2846691.
Andrieu JM, Even P, Venet A (1986). "AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications.". AIDS research 2 (3): 163–74. PMID 3489470.
Houlgatte R, Scarmato P, el Marhomy S, et al. (1994). "HLA class II antigens and the HIV envelope glycoprotein gp120 bind to the same face of CD4.". J. Immunol. 152 (9): 4475–88. PMID 7512597.
Chirmule N, McCloskey TW, Hu R, et al. (1995). "HIV gp120 inhibits T cell activation by interfering with expression of costimulatory molecules CD40 ligand and CD80 (B71).". J. Immunol. 155 (2): 917–24. PMID 7541827.
Rowell JF, Stanhope PE, Siliciano RF (1995). "Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC.". J. Immunol. 155 (1): 473–88. PMID 7602119.
Carrington M, Harding A (1994). "Sequence analysis of two novel HLA-DMA alleles.". Immunogenetics 40 (2): 165. PMID 8026867.
Radley E, Alderton RP, Kelly A, et al. (1994). "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene organization of all six class II families in the human major histocompatibility complex.". J. Biol. Chem. 269 (29): 18834–8. PMID 8034636.
Chen YH, Böck G, Vornhagen R, et al. (1994). "HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41.". Mol. Immunol. 31 (13): 977–82. PMID 8084338.
Fling SP, Arp B, Pious D (1994). "HLA-DMA and -DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells.". Nature 368 (6471): 554–8. doi:10.1038/368554a0. PMID 8139690.
Chirmule N, Wang XP, Hu R, et al. (1994). "Envelope glycoproteins of HIV-1 interfere with T-cell-dependent B cell differentiation: role of CD4-MHC class II interaction in the effector phase of T cell help.". Cell. Immunol. 155 (1): 169–82. doi:10.1006/cimm.1994.1110. PMID 8168144.
Sanderson F, Powis SH, Kelly AP, Trowsdale J (1993). "Limited polymorphism in HLA-DM does not involve the peptide binding groove.". Immunogenetics 39 (1): 56–8. PMID 8225438.
Callahan KM, Rowell JF, Soloski MJ, et al. (1993). "HIV-1 envelope protein is expressed on the surface of infected cells before its processing and presentation to class II-restricted T lymphocytes.". J. Immunol. 151 (6): 2928–42. PMID 8376762.