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Peptide-surface association: the case of PDZ and PTB domains

Article Abstract:

Signal transduction pathways are governed by regulated protein associations such as the peptide-surface mode of association. Like other protein associations, peptide-surface association has many types. Two recently discovered ones are the so-called 'PDZ domain' and 'PTB domain.' PDZ domains are repeated sequences in the brain-specific protein PSD-95, the Drosophila septate junction protein Disks-large and the epithelial tight-junction protein ZO1. On the other hand, PTB domains are regions of 100-150 residues in the insulin receptor substrates 1 and 2 and in the adaptor protein Shc.

Author: Harrison, Stephen C.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Peptides, Cellular signal transduction

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Structure of the human transferrin receptor-transferrin complex

Article Abstract:

Cryo-electron microscopy is used to uncover the molecular structure of the formation of the human transferrin receptor-transferrin complex (TfR - Tf). The structure helps understanding the differences in the iron-release properties of free and receptor bound Tf.

Author: Harrison, Stephen C., Walz, Thomas, Yifan Cheng, Zak, Olga
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
Analysis, Usage, Transferrin, Molecular structure, Electron microscopy, Atomic properties

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Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-Dependent histone deacetylation

Article Abstract:

The association of the Sir2, Sir3, and Sir4 proteins with each other and histone tails is examined. The results suggest that Sir2 activity modulates the assembly of the SIR complex through both histone deacetylation and O-acetyl-ADP-ribose (AAR) synthesis.

Author: Walz, Thomas, Moazed, Danesh, Gunn-Guang Liou, Kruger, Ryan G., Tanny, Jason C.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
Science & research, Histones, Ribosomal proteins

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