2q5h

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{{STRUCTURE_2q5h| PDB=2q5h | SCENE= }}
{{STRUCTURE_2q5h| PDB=2q5h | SCENE= }}
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'''Crystal structure of apo-wildtype Glycyl-tRNA synthetase'''
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===Crystal structure of apo-wildtype Glycyl-tRNA synthetase===
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==Overview==
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Dominant mutations in the ubiquitous enzyme glycyl-tRNA synthetase (GlyRS), including S581L, lead to motor nerve degeneration. We have determined crystal structures of wildtype and S581L-mutant human GlyRS. The S581L mutation is approximately 50A from the active site, and yet gives reduced aminoacylation activity. The overall structures of wildtype and S581L-GlyRS, including the active site, are very similar. However, residues 567-575 of the anticodon-binding domain shift position and in turn could indirectly affect glycine binding via the tRNA or alternatively inhibit conformational changes. Reduced enzyme activity may underlie neuronal degeneration, although a dominant-negative effect is more likely in this autosomal dominant disorder.
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{{ABSTRACT_PUBMED_17544401}}
==Disease==
==Disease==
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[[Category: Oxford protein production facility]]
[[Category: Oxford protein production facility]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 01:48, 29 July 2008

Image:2q5h.png

Template:STRUCTURE 2q5h

Contents

Crystal structure of apo-wildtype Glycyl-tRNA synthetase

Template:ABSTRACT PUBMED 17544401

Disease

Known disease associated with this structure: Charcot-Marie-Tooth disease, type 2D OMIM:[600287], Neuropathy, distal hereditary motor, type V OMIM:[600287]

About this Structure

2Q5H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy., Cader MZ, Ren J, James PA, Bird LE, Talbot K, Stammers DK, FEBS Lett. 2007 Jun 26;581(16):2959-64. Epub 2007 May 29. PMID:17544401

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