2etl
From Proteopedia
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- | [[Image:2etl.gif|left|200px]] | + | [[Image:2etl.gif|left|200px]] |
- | + | ||
- | '''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)''' | + | {{Structure |
+ | |PDB= 2etl |SIZE=350|CAPTION= <scene name='initialview01'>2etl</scene>, resolution 2.400Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= UCHL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2ETL is a [ | + | 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== | ||
- | 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:// | + | 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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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, resolution 2.400Å | |||||||
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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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