Crystal structure of the murine cytomegalovirus MHC-I homolog m144.
作者： Kannan Natarajan , Ashleigh Hicks , Janet Mans , Howard Robinson , Rongjin Guan
DOI: 10.1016/J.JMB.2006.01.068
关键词:
摘要: Large DNA viruses of the herpesvirus family produce proteins that mimic host MHC-I molecules as part their immunoevasive strategy. The m144 glycoprotein, expressed by murine cytomegalovirus, is thought to be an homolog whose expression prolongs viral survival in vivo preventing natural killer cell activation. To explore structural basis this function, we have determined three-dimensional structure m144/β2-microglobulin (β2m) complex at 1.9 A resolution. This reveals canonical features including readily identifiable α1, α2, and α3 domains. unique disulfide bond links α1 helix b-sheet floor, explaining known thermal stability m144. Close juxtaposition α2 helices lack critical residues normally contribute anchoring peptide N C termini eliminates binding. region 13 amino acid residues, corresponding amino-terminal portion helix, missing electron density map, suggesting area flexibility may involved ligand
rcsb.org
elsevier.com参考文章(72)
Richard J. Whitley, Bernard Roizman, Carlos Lopez, The Human Herpesviruses ,(1993)
Daniel M. Andrews, Christopher E. Andoniou, Francesca Granucci, Paola Ricciardi-Castagnoli, Mariapia A. Degli-Esposti, Infection of dendritic cells by murine cytomegalovirus induces functional paralysis Nature Immunology. ,vol. 2, pp. 1077- 1084 ,(2001) , 10.1038/NI724
Lesley Devine, Linda Rogozinski, Olga V. Naidenko, Hilde Cheroutre, Paula B. Kavathas, The Complementarity-Determining Region-Like Loops of CD8α Interact Differently with β2-Microglobulin of the Class I Molecules H-2Kb and Thymic Leukemia Antigen, While Similarly with Their α3 Domains Journal of Immunology. ,vol. 168, pp. 3881- 3886 ,(2002) , 10.4049/JIMMUNOL.168.8.3881
Anastassis Perrakis, Richard Morris, Victor S. Lamzin, Automated protein model building combined with iterative structure refinement. Nature Structural & Molecular Biology. ,vol. 6, pp. 458- 463 ,(1999) , 10.1038/8263
Roland K. Strong, Benjamin J. McFarland, NKG2D and Related Immunoreceptors Cell Surface Receptors. ,vol. 68, pp. 281- 312 ,(2004) , 10.1016/S0065-3233(04)68008-9
Yiwei Liu, Yi Xiong, Olga V. Naidenko, Jin-huan Liu, Rongguang Zhang, Andrzej Joachimiak, Mitchell Kronenberg, Hilde Cheroutre, Ellis L. Reinherz, Jia-huai Wang, The Crystal Structure of a TL/CD8αα Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory Immunity. ,vol. 18, pp. 205- 215 ,(2003) , 10.1016/S1074-7613(03)00027-X
Zbyszek Otwinowski, Wladek Minor, Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology. ,vol. 276, pp. 307- 326 ,(1997) , 10.1016/S0076-6879(97)76066-X
Mark R. Wills, Omodele Ashiru, Matthew B. Reeves, Georgina Okecha, John Trowsdale, Peter Tomasec, Gavin W. G. Wilkinson, John Sinclair, J. G. Patrick Sissons, Human Cytomegalovirus Encodes an MHC Class I-Like Molecule (UL142) That Functions to Inhibit NK Cell Lysis Journal of Immunology. ,vol. 175, pp. 7457- 7465 ,(2005) , 10.4049/JIMMUNOL.175.11.7457
J.L. Risler, M.O. Delorme, H. Delacroix, A. Henaut, Amino acid substitutions in structurally related proteins a pattern recognition approach: Determination of a new and efficient scoring matrix Journal of Molecular Biology. ,vol. 204, pp. 1019- 1029 ,(1988) , 10.1016/0022-2836(88)90058-7
José Tormo, Kannan Natarajan, David H. Margulies, Roy A. Mariuzza, Crystal Structure of a Lectin-Like Natural Killer Cell Receptor Bound to its Mhc Class I Ligand Nature. ,vol. 402, pp. 623- 631 ,(1999) , 10.1038/45170