2oit

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Revision as of 21:05, 12 November 2007


2oit, resolution 1.65Å

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Crystal Structure of the N-terminal Domain of the Human Proto-oncogene Nup214/CAN

Contents

Overview

The mammalian nuclear pore complex (NPC) is an approximately 120-MDa, proteinaceous assembly consisting of approximately 30 proteins and is the, sole gate in the nuclear envelope. The human protooncogene Nup214 was, first identified as a target for chromosomal translocation involved in, leukemogenesis. Nup214 is located on the cytoplasmic face of the NPC and, is implicated in anchoring the cytoplasmic filaments of the NPC and, recruiting the RNA helicase Ddx19. Here, we present the crystal structure, of the human Nup214 N-terminal domain at 1.65-A resolution. The structure, reveals a seven-bladed beta-propeller followed by a 30-residue C-terminal, extended peptide segment, which folds back onto the beta-propeller and, binds to its bottom face. The beta-propeller repeats lack any recognizable, sequence motif and are distinguished by extensive insertions between the, canonical beta-strands. We propose a mechanism by which the C-terminal, peptide extension is involved in NPC assembly.

Disease

Known diseases associated with this structure: Leukemia, T-cell acute lymphoblastic OMIM:[114350], Leukemia, acute myeloid OMIM:[114350]

About this Structure

2OIT is a Single protein structure of sequence from Homo sapiens with MES as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN., Napetschnig J, Blobel G, Hoelz A, Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1783-8. Epub 2007 Jan 30. PMID:17264208

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