2etl

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[[Image:2etl.gif|left|200px]]<br /><applet load="2etl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2etl.gif|left|200px]]
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caption="2etl, resolution 2.400&Aring;" />
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'''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)'''<br />
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{{Structure
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|PDB= 2etl |SIZE=350|CAPTION= <scene name='initialview01'>2etl</scene>, resolution 2.400&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|ACTIVITY=
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|GENE= UCHL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ETL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ETL OCA].
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2ETL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ETL OCA].
==Reference==
==Reference==
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Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1., Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4675-80. Epub 2006 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16537382 16537382]
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Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1., Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4675-80. Epub 2006 Mar 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16537382 16537382]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: deubiquitinating thiol hydrolase]]
[[Category: deubiquitinating thiol hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:15 2008''

Revision as of 14:44, 20 March 2008


PDB ID 2etl

Drag the structure with the mouse to rotate
, resolution 2.400Å
Ligands:
Gene: UCHL1 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)


Contents

Overview

The ubiquitin C-terminal hydrolase UCH-L1 (PGP9.5) comprises >1% of total brain protein but is almost absent from other tissues [Wilkinson, K. D., et al. (1989) Science 246, 670-673]. Mutations in the UCH-L1 gene have been reported to be linked to susceptibility to and protection from Parkinson's disease [Leroy, E., et al. (1998) Nature 395, 451-452; Maraganore, D. M., et al. (1999) Neurology 53, 1858-1860]. Abnormal overexpression of UCH-L1 has been shown to correlate with several forms of cancer [Hibi, K., et al. (1998) Cancer Res. 58, 5690-5694]. Because the amino acid sequence of UCH-L1 is similar to that of other ubiquitin C-terminal hydrolases, including the ubiquitously expressed UCH-L3, which appear to be unconnected to neurodegenerative disease, the structure of UCH-L1 and the effects of disease associated mutations on the structure and function are of considerable importance. We have determined the three-dimensional structure of human UCH-L1 at 2.4-A resolution by x-ray crystallography. The overall fold resembles that of other ubiquitin hydrolases, including UCH-L3, but there are a number of significant differences. In particular, the geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity would appear to be impossible without substrate induced conformational rearrangements.

Disease

Known disease associated with this structure: Parkinson disease, familial OMIM:[191342]

About this Structure

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

Reference

Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1., Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4675-80. Epub 2006 Mar 13. PMID:16537382

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