- 作者: Karen Hanel; Thomas Stangler; Matthias Stoldt; Dieter Willbold
- 作者服務機構: 1 Forschungszentrum Julich, Institut f? Biologische Informationsverarbeitung (IBI-2), 52425, Julich, Germany; ; 2 Heinrich-Heine-Universitat, Institut f? Physikalische Biologie and BMFZ, 40225, Dusseldorf, Germany
- 中文摘要: --
- 英文摘要: The SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-I and ICAM-2, and common features in amino acid sequence between Χ4 and ICAM-1, suggest Χ4 to possess binding activity for the αL integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of Χ4 in virus replication and pathogenesis are discussed.
- 中文關鍵字: --
- 英文關鍵字: 7a, coronavirus, immunoglobulin fold, integrin, LFA-1, NMR structure determination, ORF8, SARS, U122, X4