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5mse

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==GFP nuclear transport receptor mimic 3B8==
==GFP nuclear transport receptor mimic 3B8==
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<StructureSection load='5mse' size='340' side='right' caption='[[5mse]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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<StructureSection load='5mse' size='340' side='right'caption='[[5mse]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5mse]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSE FirstGlance]. <br>
<table><tr><td colspan='2'>[[5mse]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSE FirstGlance]. <br>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
[[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-pi interactions between arginines and FG-phenylalanines may explain this apparent paradox. Application of these principles to redesign the surface of GFP resulted in variants that show a wide span of transit rates, ranging from 35-fold slower than wild-type to approximately 500 times faster, with the latter outpacing even naturally occurring nuclear transport receptors (NTRs). The structure of a fast and particularly FG-specific GFP(NTR) variant illustrates how NTRs can expose multiple regions for binding hydrophobic FG motifs while evading non-specific aggregation. Finally, we document that even for NTR-mediated transport, the surface-properties of the "passively carried" cargo can strikingly affect the translocation rate.
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Surface Properties Determining Passage Rates of Proteins through Nuclear Pores.,Frey S, Rees R, Schunemann J, Ng SC, Funfgeld K, Huyton T, Gorlich D Cell. 2018 Jun 28;174(1):202-217.e9. doi: 10.1016/j.cell.2018.05.045. PMID:29958108<ref>PMID:29958108</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5mse" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Green Fluorescent Protein|Green Fluorescent Protein]]
*[[Green Fluorescent Protein|Green Fluorescent Protein]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aeqvi]]
[[Category: Aeqvi]]
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[[Category: Large Structures]]
[[Category: Gorlich, D]]
[[Category: Gorlich, D]]
[[Category: Huyton, T]]
[[Category: Huyton, T]]
[[Category: Fluorescent protein]]
[[Category: Fluorescent protein]]
[[Category: Gfp nuclear transport receptor]]
[[Category: Gfp nuclear transport receptor]]

Revision as of 08:04, 21 May 2019

GFP nuclear transport receptor mimic 3B8

PDB ID 5mse

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