2l1l: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2l1l.png|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2l1l", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2l1l|  PDB=2l1l  |  SCENE=  }}  
{{STRUCTURE_2l1l|  PDB=2l1l  |  SCENE=  }}  
===NMR Solution Structure of the Phi0 PKI NES Peptide in Complex with CRM1-RanGTP===
===NMR Solution Structure of the Phi0 PKI NES Peptide in Complex with CRM1-RanGTP===
{{ABSTRACT_PUBMED_20972448}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/IPKA_HUMAN IPKA_HUMAN]] Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. [[http://www.uniprot.org/uniprot/XPO1_HUMAN XPO1_HUMAN]] Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.<ref>PMID:9323133</ref> <ref>PMID:9311922</ref> <ref>PMID:9837918</ref> <ref>PMID:14612415</ref> <ref>PMID:15574332</ref> <ref>PMID:20921223</ref> 
The line below this paragraph, {{ABSTRACT_PUBMED_20972448}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 20972448 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_20972448}}


==About this Structure==
==About this Structure==
Line 22: Line 10:


==Reference==
==Reference==
<ref group="xtra">PMID:020972448</ref><ref group="xtra">PMID:021442693</ref><references group="xtra"/>
<ref group="xtra">PMID:020972448</ref><ref group="xtra">PMID:021442693</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Madl, T.]]
[[Category: Madl, T.]]