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S-domain assembly of the signal recognition particle.
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
2003 (English)In: Curr Opin Struct Biol, ISSN 0959-440X, Vol. 13, no 1, 64-70 p.Article, review/survey (Other (popular science, discussion, etc.)) Published
Abstract [en]

The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that associates with ribosomes to mediate the targeting of membrane and secretory proteins to biological membranes. In higher eukaryotes, SRP biogenesis involves the sequential binding of SRP19 and SRP54 proteins to the S domain of 7S RNA. The recently determined crystal structures of SRP19 in complex with the S domain, and that of the ternary complex of SRP19, the S domain and the M domain of SRP54, provide insight into the molecular basis of S-domain assembly and SRP function.

Place, publisher, year, edition, pages
2003. Vol. 13, no 1, 64-70 p.
Keyword [en]
Binding Sites, Crystallography/methods, Escherichia coli/chemistry/metabolism, Humans, Macromolecular Substances, Models; Molecular, Protein Binding, Protein Conformation, Protein Structure; Secondary, Protein Structure; Tertiary, RNA; Small Cytoplasmic/chemistry/metabolism, Signal Recognition Particle/*chemistry/classification/metabolism, Species Specificity, Structure-Activity Relationship
Identifiers
URN: urn:nbn:se:umu:diva-13954PubMedID: 12581661OAI: oai:DiVA.org:umu-13954DiVA: diva2:153625
Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2011-01-13Bibliographically approved

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Sauer-Eriksson, ElisabethHainzl, Tobias
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