期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 15, 期 1, 页码 116-125出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2005.01.013
关键词
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The synthesis of secretory or integral membrane proteins can be directly coupled to their translocation across or insertion into membranes. In co-translational targeting, the translation machine, the ribosome, is transferred to the respective membrane by the signal recognition particle (SIRP) and its receptor (SIR) as soon as a signal sequence emerges. Protein synthesis can continue at the membrane, with the nascent peptide chain directly inserting into the ribosome-bound protein-conducting channel, the Sec61 complex. During the past two years, several structures have been solved by crystallography and cryo-electron microscopy that represent distinct functional states of the SIRP cycle. On this basis, the first structure-based models can be suggested that explain important aspects of protein targeting, such as the SRP-ribosome and SIRP-SR interactions.
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