MHC CLASS I PEPTIDE LOADING/

MHC I 类肽加载/

• 批准号: 8169311
• 负责人: KARIN M REINISCH
• 金额: $ 2.44万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169311
• 关键词: Accounting; Affinity; Catalytic Domain; Complex; Computer Retrieval of Information on Scientific Projects Database; Covalent Interaction; Disulfides; ERp57; Family member; Funding; Glycoproteins; Grant; Institution; Link; Major Histocompatibility Complex; Molecular Models; Oxidoreductase; Peptides; Process; Protein Disulfide Isomerase; Research; Research Personnel; Resolution; Resources; Source; Structure; Sulfhydryl Compounds; Surface; United States National Institutes of Health; molecular modeling; peptide I; tapasin

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Tapasin is a glycoprotein critical for loading major histocompatibility complex (MHC) class I molecules with high-affinity peptides. It functions within the multimeric peptide-loading complex (PLC) as a disulfide-linked, stable heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction is required to support optimal PLC activity. We have solved the 2.6 A resolution structure of the tapasin-ERp57 core of the PLC. The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate. Mutational analysis identified a conserved surface on tapasin that interacted with MHC class I molecules and was critical for peptide loading and editing functions of the tapasin-ERp57 heterodimer. By combining the tapasin-ERp57 structure with those of other defined PLC components, we present a molecular model that illuminates the processes involved in MHC class I peptide loading.

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