Structure of the conserved GTPase domain of the signal recognition particle
Article Abstract:
The structure of the nucleotide-free form of the NG fragment of the protein subunit of the signal-recognition particle is described. A compact network of interactions which may stabilize the nucleotide-free protein is formed by the side chains of the empty active-site pocket. Structurally similar N and G domains are present in the SR-alpha subunit. It appears that the N domain senses or controls the nucleotide occupancy of the GTPase domain.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Substrate twinning activates the signal recognition particle and its receptor
Article Abstract:
As nascent proteins emerge from the ribosome, signal sequences are recognized by the signal recognition particle, which associates with its receptor. Signal recognition particle binds to signal sequences of membrane and secretory proteins, as they emerge from the ribosome during translation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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Eisosomes mark static sites of endocytosis
Article Abstract:
Large immobile protein assemblies called eisosomes that mark endocytic sites at the plasma membrane are described. These structures colocalize with sites of protein and lipid endocytosis and their components genetically interact with known endocytic effectors.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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