1U58

Crystal structure of the murine cytomegalovirus MHC-I homolog m144

1U58 の概要

• エントリーDOI: 10.2210/pdb1u58/pdb
• 分子名称: MHC-I homolog m144, beta-2-microglobulin (3 entities in total)
• 機能のキーワード: mcmv, mhc-i homolog, m144, beta-2m, immune system
• 由来する生物種: Murid herpesvirus 1 (Murine cytomegalovirus); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40011.81

構造登録者

Natarajan, K.,Hicks, A.,Robinson, H.,Guan, R.,Margulies, D.H. (登録日: 2004-07-27, 公開日: 2005-07-19, 最終更新日: 2024-11-13)

主引用文献

Natarajan, K.,Hicks, A.,Mans, J.,Robinson, H.,Guan, R.,Mariuzza, R.A.,Margulies, D.H.
Crystal structure of the murine cytomegalovirus MHC-I homolog m144.
J.Mol.Biol., 358:157-171, 2006

PubMed Abstract: Large DNA viruses of the herpesvirus family produce proteins that mimic host MHC-I molecules as part of their immunoevasive strategy. The m144 glycoprotein, expressed by murine cytomegalovirus, is thought to be an MHC-I homolog whose expression prolongs viral survival in vivo by preventing natural killer cell activation. To explore the structural basis of this m144 function, we have determined the three-dimensional structure of an m144/beta2-microglobulin (beta2m) complex at 1.9A resolution. This structure reveals the canonical features of MHC-I molecules including readily identifiable alpha1, alpha2, and alpha3 domains. A unique disulfide bond links the alpha1 helix to the beta-sheet floor, explaining the known thermal stability of m144. Close juxtaposition of the alpha1 and alpha2 helices and the lack of critical residues that normally contribute to anchoring the peptide N and C termini eliminates peptide binding. A region of 13 amino acid residues, corresponding to the amino-terminal portion of the alpha2 helix, is missing in the electron density map, suggesting an area of structural flexibility that may be involved in ligand binding.

PubMed: 16500675
DOI: 10.1016/j.jmb.2006.01.068

実験手法

X-RAY DIFFRACTION (1.9 Å)