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| {{STRUCTURE_1xks| PDB=1xks | SCENE= }} | | {{STRUCTURE_1xks| PDB=1xks | SCENE= }} |
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| '''The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins'''
| | ===The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15557116}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15557116 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15557116}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta-propeller]] | | [[Category: Beta-propeller]] |
| [[Category: Helical insertion]] | | [[Category: Helical insertion]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:09:34 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:58:03 2008'' |