1KOH

THE CRYSTAL STRUCTURE AND MUTATIONAL ANALYSIS OF A NOVEL RNA-BINDING DOMAIN FOUND IN THE HUMAN TAP NUCLEAR MRNA EXPORT FACTOR

Summary for 1KOH

• Entry DOI: 10.2210/pdb1koh/pdb
• Related: 1FO1 1FT8 1KOO
• Descriptor: TIP ASSOCIATING PROTEIN (1 entity in total)
• Functional Keywords: mrna export factor, constitutive transport element (cte) ribonucleoprotein (rnp) and leucine rich repeat (lrr) domains, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleoplasm: Q9UBU9
• Total number of polymer chains: 4
• Total formula weight: 125931.39

Authors

Ho, D.N.,Coburn, G.A.,Kang, Y.,Cullen, B.R.,Georgiadis, M.M. (deposition date: 2001-12-20, release date: 2002-02-27, Last modification date: 2023-08-16)

Primary citation

Ho, D.N.,Coburn, G.A.,Kang, Y.,Cullen, B.R.,Georgiadis, M.M.
The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.
Proc.Natl.Acad.Sci.USA, 99:1888-1893, 2002

PubMed Abstract: The Tap protein mediates the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element (CTE). Previously, the structures of individual Tap subdomains, including ribonucleoprotein and leucine-rich repeat domains, have been described. Here, we report the crystal structure of a functional CTE RNA-binding domain of human Tap, including the N-terminal arm of the ribonucleoprotein domain and interdomain linking polypeptide. To identify residues that interact with the CTE, we have introduced 38 alanine substitutions for surface residues in the Tap CTE-binding domain and tested these mutants for their ability to support CTE-dependent nuclear RNA export and CTE binding. Four residues that cluster on a concave surface in the leucine-rich repeat domain were found to be critical for CTE binding and define a CTE-interacting surface on this domain. The second critical CTE-interacting surface on Tap is defined by three previously identified residues on the surface of the ribonucleoprotein domain. The structural and mutational data define a novel RNA-binding site on the Tap protein.

PubMed: 11854490
DOI: 10.1073/pnas.042698599

Experimental method

X-RAY DIFFRACTION (3.8 Å)