Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3
Article Abstract:
A study expresses and crystallizes a soluble form of H2-M3 with a formylated nonamer peptide, fMYFINILTL, and determines the structure by X-ray crystallography. M3 refines at a resolution of 2.1 angstrom, and its overall structure resembles a class la MHC molecule, but it differs in the peptide binding groove. The A pocket is closed, and the peptide chain is connected to the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
Article Abstract:
The 2.3 angstrom crystal structure of the Gp31 protein reveals that its tertiary and quaternary structures are similar to those of GroES in spite of only a 14% sequence similarity between the two proteins. However, Gp31 exhibits a series of structural adaptations which will increase the size and hydrophilicity of the 'Anfinsen cage,' the cavity which is the site of the chaperonin-assisted protein folding reaction.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Metal import through microbial membranes
Article Abstract:
The Gram-negative cell envelope defines four compartments within the bacterial cell- outer membrane, periplasm, cytoplasmic membrane, and cytoplasm. The transport systems of Gram-negative bacteria focuses on structural and mechanistic principles of active import systems of E. coil for metal chelates. Functional models that are derived from structural data are discussed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
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