期刊
JOURNAL OF IMMUNOLOGY
卷 174, 期 6, 页码 3501-3507出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.174.6.3501
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资金
- NCI NIH HHS [CA048115] Funding Source: Medline
- NIAID NIH HHS [AI50263, AI40617] Funding Source: Medline
- NIDDK NIH HHS [DK54451] Funding Source: Medline
- NIGMS NIH HHS [GM56008] Funding Source: Medline
The mouse thymic leukemia (TL) Ag is a nonclassical MHC class I molecule that binds with higher affinity to CD8alphaalpha than CD8alphabeta. The interaction of CD8alphaalpha with TL is important for lymphocyte regulation in the intestine. Therefore, we studied the molecular basis for TL Ag binding to CD8alphaalpha. The stronger affinity of the TL Ag for CD8alphaalpha is largely mediated by three amino acids on exposed loops of the conserved alpha(3) domain. Mutant classical class I molecules substituted with TL Ag amino acids at these positions mimic the ability to interact with CD8alphaalpha and modulate lymphocyte function. These data indicate that small changes in the alpha(3) domain of class I molecules potentially can have profound physiologic consequences.
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