2gj7

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Template:STRUCTURE 2gj7

Contents

Crystal Structure of a gE-gI/Fc complex

Template:ABSTRACT PUBMED 16646632

Disease

[IGHG1_HUMAN] Defects in IGHG1 are a cause of multiple myeloma (MM) [MIM:254500]. MM is a malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia. Note=A chromosomal aberration involving IGHG1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3; translocation t(6;14)(p25;q32) with IRF4.

Function

[VGLE_HHV11] In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells (By similarity). In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips.[1][2] The heterodimer gE/gI serves as a receptor for the Fc part of host IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus be involved in anti-HSV antibodies bipolar bridging, followed by intracellular endocytosis and degradation, thereby interfering with host IgG-mediated immune responses.[3][4]

About this Structure

2gj7 is a 4 chain structure with sequence from Cricetulus griseus, Homo sapiens and Human herpesvirus 1. Full crystallographic information is available from OCA.

Reference

  • Sprague ER, Wang C, Baker D, Bjorkman PJ. Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a mechanism for antibody bipolar bridging. PLoS Biol. 2006 Jun;4(6):e148. Epub 2006 May 2. PMID:16646632 doi:10.1371/journal.pbio.0040148
  1. ↑ Johnson DC, Frame MC, Ligas MW, Cross AM, Stow ND. Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J Virol. 1988 Apr;62(4):1347-54. PMID:2831396
  2. ↑ Sprague ER, Martin WL, Bjorkman PJ. pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J Biol Chem. 2004 Apr 2;279(14):14184-93. Epub 2004 Jan 20. PMID:14734541 doi:10.1074/jbc.M313281200
  3. ↑ Johnson DC, Frame MC, Ligas MW, Cross AM, Stow ND. Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI. J Virol. 1988 Apr;62(4):1347-54. PMID:2831396
  4. ↑ Sprague ER, Martin WL, Bjorkman PJ. pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J Biol Chem. 2004 Apr 2;279(14):14184-93. Epub 2004 Jan 20. PMID:14734541 doi:10.1074/jbc.M313281200

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