2aiv: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="2aiv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aiv" /> '''Multiple conformations in the ligand-binding...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2aiv.gif|left|200px]]<br /><applet load="2aiv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2aiv" />
'''Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116P'''<br />


==Overview==
==Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116P==
The yeast nucleoporin Nup116p plays an important role in mRNA export and, protein transport. We have determined the solution structure of the, C-terminal 147 residues of this protein, the region responsible for, targeting the protein to the nuclear pore complex (NPC). The structure of, Nup116p-C consists of a large beta-sheet sandwiched against a smaller one, flanked on both sides by alpha-helical stretches, similar to the structure, of its human homolog, NUP98. In unliganded form, Nup116p-C exhibits, evidence of exchange among multiple conformations, raising the intriguing, possibility that it may adopt distinct conformations when bound to, different partners in the NPC. We have additionally shown that a peptide, from the N terminus of the nucleoporin Nup145p-C binds Nup116p-C. This, previously unknown interaction may explain the unusual asymmetric, localization pattern of Nup116p in the NPC. Strikingly, the exchange, phenomenon observed in the unbound state is greatly reduced in the, corresponding spectra of peptide-bound Nup116p-C, suggesting that the, binding interaction stabilizes the domain conformation. This study offers, a high resolution view of a yeast nucleoporin structural domain and may, provide insights into NPC architecture and function.
<StructureSection load='2aiv' size='340' side='right'caption='[[2aiv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2aiv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AIV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aiv OCA], [https://pdbe.org/2aiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aiv RCSB], [https://www.ebi.ac.uk/pdbsum/2aiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aiv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NU116_YEAST NU116_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport.<ref>PMID:8044840</ref> <ref>PMID:8524308</ref> <ref>PMID:9463388</ref> <ref>PMID:9891088</ref> <ref>PMID:10891509</ref> <ref>PMID:10952996</ref> <ref>PMID:11071906</ref> <ref>PMID:10801828</ref> <ref>PMID:11387327</ref> <ref>PMID:11689687</ref> <ref>PMID:11104765</ref> <ref>PMID:12372823</ref> <ref>PMID:12604785</ref> <ref>PMID:15039779</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/2aiv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aiv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2AIV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AIV OCA].
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
 
== References ==
==Reference==
<references/>
Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p., Robinson MA, Park S, Sun ZY, Silver PA, Wagner G, Hogle JM, J Biol Chem. 2005 Oct 21;280(42):35723-32. Epub 2005 Aug 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16105837 16105837]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Hogle J]]
[[Category: Hogle, J.]]
[[Category: Park S]]
[[Category: Park, S.]]
[[Category: Robinson MA]]
[[Category: Robinson, M.A.]]
[[Category: Silver P]]
[[Category: Silver, P.]]
[[Category: Sun Z-YJ]]
[[Category: Sun, Z-Y.J.]]
[[Category: Wagner G]]
[[Category: Wagner, G.]]
[[Category: beta sandwich]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:09:16 2007''

Latest revision as of 09:37, 1 May 2024

Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116PMultiple conformations in the ligand-binding site of the yeast nuclear pore targeting domain of NUP116P

Structural highlights

2aiv is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NU116_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Fabre E, Boelens WC, Wimmer C, Mattaj IW, Hurt EC. Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell. 1994 Jul 29;78(2):275-89. PMID:8044840
  2. ↑ Sharma K, Fabre E, Tekotte H, Hurt EC, Tollervey D. Yeast nucleoporin mutants are defective in pre-tRNA splicing. Mol Cell Biol. 1996 Jan;16(1):294-301. PMID:8524308
  3. ↑ Bailer SM, Siniossoglou S, Podtelejnikov A, Hellwig A, Mann M, Hurt E. Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. EMBO J. 1998 Feb 16;17(4):1107-19. PMID:9463388 doi:http://dx.doi.org/10.1093/emboj/17.4.1107
  4. ↑ Seedorf M, Damelin M, Kahana J, Taura T, Silver PA. Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol. 1999 Feb;19(2):1547-57. PMID:9891088
  5. ↑ Ho AK, Shen TX, Ryan KJ, Kiseleva E, Levy MA, Allen TD, Wente SR. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol. 2000 Aug;20(15):5736-48. PMID:10891509
  6. ↑ Strasser K, Bassler J, Hurt E. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J Cell Biol. 2000 Aug 21;150(4):695-706. PMID:10952996
  7. ↑ Stage-Zimmermann T, Schmidt U, Silver PA. Factors affecting nuclear export of the 60S ribosomal subunit in vivo. Mol Biol Cell. 2000 Nov;11(11):3777-89. PMID:11071906
  8. ↑ Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000 Aug 4;275(31):23540-8. PMID:10801828 doi:http://dx.doi.org/10.1074/jbc.M001963200
  9. ↑ Allen NP, Huang L, Burlingame A, Rexach M. Proteomic analysis of nucleoporin interacting proteins. J Biol Chem. 2001 Aug 3;276(31):29268-74. Epub 2001 May 31. PMID:11387327 doi:http://dx.doi.org/10.1074/jbc.M102629200
  10. ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
  11. ↑ Strawn LA, Shen T, Wente SR. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J Biol Chem. 2001 Mar 2;276(9):6445-52. Epub 2000 Dec 4. PMID:11104765 doi:http://dx.doi.org/10.1074/jbc.M008311200
  12. ↑ Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. J Biol Chem. 2002 Dec 27;277(52):50597-606. Epub 2002 Oct 7. PMID:12372823 doi:10.1074/jbc.M209037200
  13. ↑ Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2450-5. Epub 2003 Feb 25. PMID:12604785 doi:10.1073/pnas.0437902100
  14. ↑ Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol. 2004 Mar;6(3):197-206. Epub 2004 Feb 22. PMID:15039779 doi:10.1038/ncb1097
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2aiv&oldid=4135306"