Structures of PLC captured at distinct assembly states provide mechanistic insight into the recruitment and release of MHC-I. Our work defines the molecular symbiosis of an ABC transporter and an endoplasmic reticulum chaperone network in MHC-I assembly and provides insight into the onset of the ...
Here, we determine the crystal structure of MILL2 at 2.15 resolution, revealing an organization similar to classical MHC class I. However, the α1-α2 domains are not tightly fixed on the α3-βm domains, indicating unusual interdomain flexibility. The groove between the two helices in the ...
some γδ TCRs deviate from this paradigm—for example, binding underneath or to the side of the antigen-binding platform of their MHC-I-like ligands4,10,12. The MR1-reactive G83.C4 γδ TCR and the AF-7 αβ TCR conform to this general pattern, binding to the side ...
Candon, S., Margulies, D.H. (2004). MHC: Structure and Function. In: Wilkes, D.S., Burlingham, W.J. (eds) Immunobiology of Organ Transplantation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8999-4_3 Download citation ...
In addition to its role as a sensor of protein folding, UGGT contributes to the maturation of the major histocompatibility complex of class 1 molecules (MHC1), ensuring that a high-affinity peptide has been loaded onto the MHC1 heavy chains (28, 29). The MHC1 is composed of MHC-encoded...
Additional file 10: of DynaDom: structure-based prediction of T cell receptor inter-domain and T cell receptor-peptide-MHC (class I) association angles T-cell receptors (TCR) play an important role in the adaptive immune system as they recognize pathogen- or cancer-based epitopes and thus ini...
The major histocompatibility complex (MHC) class I homolog, MICA, is a stress-inducible ligand for NKG2D, a C-type lectin-like activating immunoreceptor. The crystal structure of this ligand-receptor complex that we report here reveals an NKG2D homodimer bound to a MICA monomer in an interaction...
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel β-...
& Turk, D. Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J. 18, 793–803 (1999). Article PubMed PubMed Central Google Scholar Molina, F., Bouanani, M., Pau, B. & ...
Bulmer, J.N., Morrison, L. and Smith, J.C.: Expression of class II MHC gene products by macrophages in human uteroplacental tissue. Immunology63: 707–714, 1988. PubMedCASGoogle Scholar Bulmer, J.N., Thrower, S. and Wells, M.: Expression of epidermal growth factor receptor and transf...