This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

6b4f

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 17:09, 20 November 2019

Crystal structure of human Gle1 CTD-Nup42 GBM complex

Structural highlights

6b4f is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	GLE1, GLE1L (HUMAN), NUPL2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[GLE1_HUMAN] Lethal arthrogryposis - anterior horn cell disease;Lethal congenital contracture syndrome type 1. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[GLE1_HUMAN] Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The nuclear pore complex (NPC) controls the passage of macromolecules between the nucleus and cytoplasm, but how the NPC directly participates in macromolecular transport remains poorly understood. In the final step of mRNA export, the DEAD-box helicase DDX19 is activated by the nucleoporins Gle1, Nup214, and Nup42 to remove Nxf1*Nxt1 from mRNAs. Here, we report crystal structures of Gle1*Nup42 from three organisms that reveal an evolutionarily conserved binding mode. Biochemical reconstitution of the DDX19 ATPase cycle establishes that human DDX19 activation does not require IP6, unlike its fungal homologs, and that Gle1 stability affects DDX19 activation. Mutations linked to motor neuron diseases cause decreased Gle1 thermostability, implicating nucleoporin misfolding as a disease determinant. Crystal structures of human Gle1*Nup42*DDX19 reveal the structural rearrangements in DDX19 from an auto-inhibited to an RNA-binding competent state. Together, our results provide the foundation for further mechanistic analyses of mRNA export in humans.

Structural and functional analysis of mRNA export regulation by the nuclear pore complex.,Lin DH, Correia AR, Cai SW, Huber FM, Jette CA, Hoelz A Nat Commun. 2018 Jun 13;9(1):2319. doi: 10.1038/s41467-018-04459-3. PMID:29899397^[4]

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

References

↑ Kendirgi F, Barry DM, Griffis ER, Powers MA, Wente SR. An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export. J Cell Biol. 2003 Mar 31;160(7):1029-40. doi: 10.1083/jcb.200211081. PMID:12668658 doi:http://dx.doi.org/10.1083/jcb.200211081
↑ Kendirgi F, Rexer DJ, Alcazar-Roman AR, Onishko HM, Wente SR. Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA. Mol Biol Cell. 2005 Sep;16(9):4304-15. Epub 2005 Jul 6. PMID:16000379 doi:http://dx.doi.org/E04-11-0998
↑ Watkins JL, Murphy R, Emtage JL, Wente SR. The human homologue of Saccharomyces cerevisiae Gle1p is required for poly(A)+ RNA export. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6779-84. PMID:9618489
↑ Lin DH, Correia AR, Cai SW, Huber FM, Jette CA, Hoelz A. Structural and functional analysis of mRNA export regulation by the nuclear pore complex. Nat Commun. 2018 Jun 13;9(1):2319. doi: 10.1038/s41467-018-04459-3. PMID:29899397 doi:http://dx.doi.org/10.1038/s41467-018-04459-3

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6b4f"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Gle1 CTD-Nup42 GBM complex==
-<StructureSection load='6b4f' size='340' side='right' caption='[[6b4f]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+<StructureSection load='6b4f' size='340' side='right'caption='[[6b4f]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6b4f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B4F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B4F FirstGlance]. <br>
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Cai, S W]]
 [[Category: Correia, A R]]

6b4f

From Proteopedia

Revision as of 17:09, 20 November 2019

Crystal structure of human Gle1 CTD-Nup42 GBM complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox