Crystal structure of the complex between human CD80-alpha-alpha and HLA-A2
Article Abstract:
Recent research has looked at the crystal structure of a complex between CD8-alpha-alpha and the human major histocompatability complex (MHC) molecule HLA-A2, which is linked with peptide. It was found that the binding of CD8 to MHC is consistent with an avidity-based contribution from CD8 to TCR-peptide-MHC interactions. This can be concluded from the fact that the binding sites of CD8 and the T-cell antigen receptor to MHC class 1 are separate in spatial terms but need similar orientations of the MHC molecule in relation to the target cell surface.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Crystal structure at 2.8 angstrom resolution of a soluble form of the cell adhesion molecule CD2
Article Abstract:
The topology of the crystal structure of the soluble cell adhesion molecule T lymphocyte antigen CD2 contains two immunoglobulin-like domains and may be a model for that of the immunoglobulin superfamily. This topology resembles the first two domains of CD4, but a flexible linker region maintains the relative domain orientation. This flexibility may facilitate docking of molecules on opposing cell surfaces. CD2 is longer than CD4 though it contains fewer amino acids, and this may increase exposure to the putative binding ligand.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Cutting complexity down to size
Article Abstract:
The proteasome is involved in many biological processes in plants, animals and archaebacteria and is the main complex for protein degradation. The molecular and crystal structure of the yeast 20S proteasome has been determined and the structure provides clues as to how protein degradation is carried out. Analysis shows that the molecule is composed of 28 protein chains. Suggestions as to how the molecular conglomerate may work are presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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