2oit
From Proteopedia
(New page: 200px<br /> <applet load="2oit" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oit, resolution 1.65Å" /> '''Crystal Structure o...) |
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| - | [[Image:2oit.gif|left|200px]]<br /> | + | [[Image:2oit.gif|left|200px]]<br /><applet load="2oit" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2oit" size=" | + | |
caption="2oit, resolution 1.65Å" /> | caption="2oit, resolution 1.65Å" /> | ||
'''Crystal Structure of the N-terminal Domain of the Human Proto-oncogene Nup214/CAN'''<br /> | '''Crystal Structure of the N-terminal Domain of the Human Proto-oncogene Nup214/CAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mammalian nuclear pore complex (NPC) is an approximately 120-MDa | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2OIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:18:57 2008'' |
Revision as of 16:18, 21 February 2008
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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 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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