1uxw: Difference between revisions

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[[Image:1uxw.png|left|200px]]
{{STRUCTURE_1uxw|  PDB=1uxw  |  SCENE=  }}  
{{STRUCTURE_1uxw|  PDB=1uxw  |  SCENE=  }}  
===CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2) OF EPSTEIN-BARR VIRUS===
{{ABSTRACT_PUBMED_15537660}}


===CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2) OF EPSTEIN-BARR VIRUS===
==Disease==
[[http://www.uniprot.org/uniprot/1B27_HUMAN 1B27_HUMAN]] Defects in HLA-B are a cause of susceptibility to spondyloarthropathy type 1 (SPDA1) [MIM:[http://omim.org/entry/106300 106300]]. It is a chronic rheumatic disease with multifactorial inheritance. It includes a spectrum of related disorders comprising ankylosing spondylitis, a subset of psoriatic arthritis, reactive arthritis (e.g. Reiter syndrome), arthritis associated with inflammatory bowel disease and undifferentiated spondyloarthropathy. These disorders may occur simultaneously or sequentially in the same patient, probably representing various phenotypic expressions of the same disease. Ankylosing spondylitis is the form of rheumatoid arthritis affecting the spine and is considered the prototype of seronegative spondyloarthropathies. It produces pain and stiffness as a result of inflammation of the sacroiliac, intervertebral, and costovertebral joints. Note=In the Greek Cypriot population, a restricted number of HLA-B27 subtypes are associated with ankylosing spondylitis and other B27-related diseases and an elevated frequency of the B*2702 allele in ankylosing spondylitis patients is identified. The allele B*2707 seems to have a protective role in this population because it was found only in the healthy controls.<ref>PMID:15603872</ref>


{{ABSTRACT_PUBMED_15537660}}
==Function==
[[http://www.uniprot.org/uniprot/1B27_HUMAN 1B27_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/LMP2_EBV LMP2_EBV]] Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs.<ref>PMID:8290598</ref><ref>PMID:9768760</ref>  Isoform LMP2B may be a negative regulator of isoform LMP2A.<ref>PMID:8290598</ref><ref>PMID:9768760</ref>


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:015537660</ref><ref group="xtra">PMID:014734527</ref><references group="xtra"/>
<ref group="xtra">PMID:015537660</ref><ref group="xtra">PMID:014734527</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Fiorillo, M T.]]
[[Category: Fiorillo, M T.]]

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