This title appears in the Scientific Report :
2006
Please use the identifier:
http://dx.doi.org/10.1007/s11373-005-9043-9 in citations.
Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains
Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains
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...
Saved in:
Personal Name(s): | Haenel, K. |
---|---|
Stangler, T. / Stoldt, M. / Willbold, D. | |
Contributing Institute: |
Biologische Strukturforschung; IBI-2 |
Published in: | Journal of biomedical science, 13 (2006) S. 281 - 293 |
Imprint: |
London
BioMed Central
2006
|
Physical Description: |
281 - 293 |
PubMed ID: |
16328780 |
DOI: |
10.1007/s11373-005-9043-9 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems |
Series Title: |
Journal of Biomedical Science
13 |
Subject (ZB): | |
Publikationsportal JuSER |
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-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed. |