Correlated mutations in the HLA class II molecule

✍ Scribed by Anna M. Nilsson; Mihirinie Wijaywardene; George Gkoutos; Keith M. Wilson; Nelson Fernández; Christopher A. Reynolds

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 360 KB
• Volume: 73
• Category: Article
• ISSN: 0020-7608
• DOI: 10.1002/(sici)1097-461x(1999)73:2<85::aid-qua4>3.0.co;2-o

✦ Synopsis

A correlated mutation analysis was performed on aligned sequences of

Ž

. the human leukocyte antigen HLA HLA-DR, HLA-DP, and HLA-DQ class II receptors with a view to understanding their molecular associations, particularly those involving their ␣ and ␤ domains. The analysis was carried out on 23 HLA-DR alleles, 12 DP alleles, and 24 DQ alleles; the analysis was also carried out on the global alignment of the DR, DP, and DQ alleles. These analyses identified 13, 18, 26, and 27 correlated mutations, respectively. Between 72 and 85% of the correlated mutations were found to occur at domain interfaces within the ␣ or ␤ chain, at the interface of the ␣␤ heterodimer, or at Ž . the interface of the ␣␤ dimer of heterodimers. These results are discussed in the light 2 of recent results that have shown that the HLA class II receptor forms temperaturedependent dimers of dimers on the surface of living cells.