1NEZ

The Crystal Structure of a TL/CD8aa Complex at 2.1A resolution:Implications for Memory T cell Generation, Co-receptor Preference and Affinity

Summary for 1NEZ

• Entry DOI: 10.2210/pdb1nez/pdb
• Descriptor: H-2 class I histocompatibility antigen, TLA(C) alpha chain, Beta-2-microglobulin, T-cell surface glycoprotein CD8 alpha chain, ... (5 entities in total)
• Functional Keywords: immune system
• Total number of polymer chains: 4
• Total formula weight: 73044.29

Authors

Liu, Y.,Xiong, Y.,Naidenko, O.V.,Liu, J.H.,Zhang, R.,Joachimiak, A.,Kronenberg, M.,Cheroutre, H.,Reinherz, E.L.,Wang, J.H. (deposition date: 2002-12-12, release date: 2003-04-08, Last modification date: 2020-07-29)

Primary citation

Liu, Y.,Xiong, Y.,Naidenko, O.V.,Liu, J.H.,Zhang, R.,Joachimiak, A.,Kronenberg, M.,Cheroutre, H.,Reinherz, E.L.,Wang, J.H.
The Crystal Structure of a TL/CD8alphaalpha Complex at 2.1 A resolution: Implications for modulation of T cell activation and memory
Immunity, 18:205-215, 2003

PubMed Abstract: TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8alphaalpha. To investigate how the TL/CD8alphaalpha interaction influences TCR signaling, we characterized the structure of the TL/CD8alphaalpha complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8alphaalpha interaction is strengthened through subtle structure changes in the TL alpha3 domain. Thus, TL functions to sequester and redirect CD8alphaalpha away from the TCR, modifying lck-dependent signaling.

PubMed: 12594948
DOI: 10.1016/S1074-7613(03)00027-X

Experimental method

X-RAY DIFFRACTION (2.1 Å)