1oai
From Proteopedia
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| - | [[Image:1oai.jpg|left|200px]] | + | [[Image:1oai.jpg|left|200px]] |
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| - | '''COMPLEX BETWEEN TAP UBA DOMAIN AND FXFG NUCLEOPORIN PEPTIDE''' | + | {{Structure |
| + | |PDB= 1oai |SIZE=350|CAPTION= <scene name='initialview01'>1oai</scene>, resolution 1.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''COMPLEX BETWEEN TAP UBA DOMAIN AND FXFG NUCLEOPORIN PEPTIDE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OAI is a [ | + | 1OAI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAI OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution., Grant RP, Neuhaus D, Stewart M, J Mol Biol. 2003 Feb 21;326(3):849-58. PMID:[http:// | + | Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution., Grant RP, Neuhaus D, Stewart M, J Mol Biol. 2003 Feb 21;326(3):849-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12581645 12581645] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: nucleoporin]] | [[Category: nucleoporin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:08 2008'' |
Revision as of 11:08, 20 March 2008
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| , resolution 1.00Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX BETWEEN TAP UBA DOMAIN AND FXFG NUCLEOPORIN PEPTIDE
Contents |
Overview
The mRNA nuclear export function of Tap/NXF1 requires interactions with nuclear pore proteins (nucleoporins) that contain characteristic Phe-Gly repeats based on FG, GLFG or FxFG cores separated by hydrophilic linkers. FG-nucleoporins bind the two most C-terminal domains of Tap, which have NTF2 and UBA folds, respectively. We used a combination of NMR and X-ray crystallography to define the interaction interface between Tap UBA and FxFG nucleoporins and show that it involves primarily the two aromatic rings of the FxFG core that bind in a hydrophobic surface depression centred on Tap Cys588. NMR evidence indicates that the same depression mediates the binding of GLFG nucleoporins, which we confirmed by demonstrating competition between the two classes of repeat for binding to Tap UBA. Moreover, modification of Cys588 reduced the binding of Tap UBA to both GLFG and FxFG nucleoporins as well as to nuclear envelopes. These data underscore the central role of the conserved FG-nucleoporin repeat cores in binding to Tap UBA and indicate that functional differences between different classes of nucleoporins depend more on their spatial distribution in nuclear pores than on their binding to different sites on Tap UBA.
Disease
Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[170260]
About this Structure
1OAI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution., Grant RP, Neuhaus D, Stewart M, J Mol Biol. 2003 Feb 21;326(3):849-58. PMID:12581645
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