1jj7

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Template:STRUCTURE 1jj7

Contents 1 Crystal Structure of the C-terminal ATPase domain of human TAP1 2 Disease 3 Function 4 About this Structure 5 Reference

Crystal Structure of the C-terminal ATPase domain of human TAP1

Template:ABSTRACT PUBMED 11532960

Disease

[TAP1_HUMAN] Defects in TAP1 are a cause of bare lymphocyte syndrome type 1 (BLS1) [MIM:604571]; also called HLA class I deficiency. BLS1 is a class I antigen deficiency that is not accompanied by particular pathologic manifestations during the first years of life. Systemic infections have not been described. Chronic bacterial infections, often beginning in the first decade of life, are restricted to the respiratory tract.^[1]

Function

[TAP1_HUMAN] Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.

About this Structure

1jj7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

• Gaudet R, Wiley DC. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. 2001 Sep 3;20(17):4964-72. PMID:11532960 doi:10.1093/emboj/20.17.4964

1. ↑ Furukawa H, Murata S, Yabe T, Shimbara N, Keicho N, Kashiwase K, Watanabe K, Ishikawa Y, Akaza T, Tadokoro K, Tohma S, Inoue T, Tokunaga K, Yamamoto K, Tanaka K, Juji T. Splice acceptor site mutation of the transporter associated with antigen processing-1 gene in human bare lymphocyte syndrome. J Clin Invest. 1999 Mar;103(5):755-8. PMID:10074494 doi:10.1172/JCI5335