4ye6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The crystal structure of the intact human GlnRS== | ==The crystal structure of the intact human GlnRS== | ||
<StructureSection load='4ye6' size='340' side='right' caption='[[4ye6]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4ye6' size='340' side='right'caption='[[4ye6]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ye6]] is a 1 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=4YE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YE6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ye6]] is a 1 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=4YE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YE6 FirstGlance]. <br> | ||
| Line 22: | Line 22: | ||
</div> | </div> | ||
<div class="pdbe-citations 4ye6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ye6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 31: | ||
[[Category: Glutamine--tRNA ligase]] | [[Category: Glutamine--tRNA ligase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Ling, J]] | [[Category: Ling, J]] | ||
[[Category: Ognjenovic, J]] | [[Category: Ognjenovic, J]] | ||
Revision as of 13:47, 25 December 2019
The crystal structure of the intact human GlnRSThe crystal structure of the intact human GlnRS
Structural highlights
Disease[SYQ_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Function[SYQ_HUMAN] Plays a critical role in brain development.[1] Publication Abstract from PubMedCytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons. Compound heterozygous mutations in GlnRS cause severe brain disorders by a poorly understood mechanism. Herein, we present crystal structures of the wild type and two pathological mutants of human GlnRS, which reveal, for the first time, the domain organization of the intact enzyme and the structure of the functionally important N-terminal domain (NTD). Pathological mutations mapping in the NTD alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme. Our results suggest that the reduced catalytic efficiency and a propensity of GlnRS mutants to misfold trigger the disease development. This report broadens the spectrum of brain pathologies elicited by protein misfolding and provides a paradigm for understanding the role of mutations in aminoacyl-tRNA synthetases in neurological diseases. The crystal structure of human GlnRS provides basis for the development of neurological disorders.,Ognjenovic J, Wu J, Matthies D, Baxa U, Subramaniam S, Ling J, Simonovic M Nucleic Acids Res. 2016 Feb 10. pii: gkw082. PMID:26869582[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||