1xks
From Proteopedia
The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins
Overview
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nup133 beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex.
About this Structure
1XKS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex., Berke IC, Boehmer T, Blobel G, Schwartz TU, J Cell Biol. 2004 Nov 22;167(4):591-7. PMID:15557116 Page seeded by OCA on Sat May 3 15:09:34 2008
