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2bpt

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Revision as of 16:47, 25 December 2014

STRUCTURE OF THE NUP1P:KAP95P COMPLEX

Structural highlights

2bpt is a 2 chain structure with sequence from Saccharomyces cerevisiae. The January 2007 RCSB PDB Molecule of the Month feature on Importins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2bku
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[IMB1_YEAST] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.^[1] [NUP1_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). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10]

Evolutionary Conservation

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

Publication Abstract from PubMed

Macromolecules are transported across the nuclear envelope most frequently by karyopherin/importin-beta superfamily members that are constructed from HEAT repeats. Transport of Kap95p (yeast importin-beta), the principal carrier for protein import, through nuclear pore complexes is facilitated by interactions with nucleoporins containing FG repeats. However, Nup1p interacts more strongly with Kap95p than other FG-nucleoporins. To establish the basis of this increased affinity, we determined the structure of Kap95p complexed with Nup1p residues 963-1076 that contain the high-affinity Kap95p binding site. Nup1p binds Kap95p at three sites between the outer A-helices of HEAT repeats 5, 6, 7 and 8. At each site, phenylalanine residues from Nup1p are buried in hydrophobic depressions between adjacent HEAT repeats. Although the Nup1p and generic FG-nucleoporin binding sites on Kap95p overlap, Nup1p binding differs markedly and has contributions from additional hydrophobic residues, together with interactions generated by the intimate contact of the linker between Nup1 residues 977-987 with Kap95p. The length and composition of this linker is crucial and suggests how differences in affinity for Kap95p both between and within FG-nucleoporins arise.

Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p.,Liu SM, Stewart M J Mol Biol. 2005 Jun 10;349(3):515-25. Epub 2005 Apr 19. PMID:15878174^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mosammaparast N, Jackson KR, Guo Y, Brame CJ, Shabanowitz J, Hunt DF, Pemberton LF. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J Cell Biol. 2001 Apr 16;153(2):251-62. PMID:11309407
↑ Solsbacher J, Maurer P, Vogel F, Schlenstedt G. Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha. Mol Cell Biol. 2000 Nov;20(22):8468-79. PMID:11046143
↑ 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
↑ Denning D, Mykytka B, Allen NP, Huang L, Al Burlingame, Rexach M. The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex. J Cell Biol. 2001 Sep 3;154(5):937-50. PMID:11535617 doi:http://dx.doi.org/10.1083/jcb.200101007
↑ 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
↑ Allen NP, Patel SS, Huang L, Chalkley RJ, Burlingame A, Lutzmann M, Hurt EC, Rexach M. Deciphering networks of protein interactions at the nuclear pore complex. Mol Cell Proteomics. 2002 Dec;1(12):930-46. PMID:12543930
↑ Gilchrist D, Mykytka B, Rexach M. Accelerating the rate of disassembly of karyopherin.cargo complexes. J Biol Chem. 2002 May 17;277(20):18161-72. Epub 2002 Feb 26. PMID:11867631 doi:http://dx.doi.org/10.1074/jbc.M112306200
↑ Pyhtila B, Rexach M. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J Biol Chem. 2003 Oct 24;278(43):42699-709. Epub 2003 Aug 12. PMID:12917401 doi:http://dx.doi.org/10.1074/jbc.M307135200
↑ 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
↑ 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
↑ Liu SM, Stewart M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p. J Mol Biol. 2005 Jun 10;349(3):515-25. Epub 2005 Apr 19. PMID:15878174 doi:10.1016/j.jmb.2005.04.003

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bpt"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2bpt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The January 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Importins''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_1 10.2210/rcsb_pdb/mom_2007_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BPT FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bku|2bku]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bku|2bku]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bpt RCSB], [http://www.ebi.ac.uk/pdbsum/2bpt PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bpt RCSB], [http://www.ebi.ac.uk/pdbsum/2bpt PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/IMB1_YEAST IMB1_YEAST]] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.<ref>PMID:11309407</ref>  [[http://www.uniprot.org/uniprot/NUP1_YEAST NUP1_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). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.<ref>PMID:11046143</ref> <ref>PMID:11387327</ref> <ref>PMID:11535617</ref> <ref>PMID:12372823</ref> <ref>PMID:12543930</ref> <ref>PMID:11867631</ref> <ref>PMID:12917401</ref> <ref>PMID:12604785</ref> <ref>PMID:15039779</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 37: @@
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Liu, S M.]]
+[[Category: Liu, S M]]
-[[Category: Stewart, M.]]
+[[Category: Stewart, M]]
 [[Category: Complex]]
 [[Category: Importin- beta]]

2bpt

From Proteopedia

Revision as of 16:47, 25 December 2014

STRUCTURE OF THE NUP1P:KAP95P COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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