This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2etl
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2etl.gif|left|200px]] | [[Image:2etl.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2etl", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2etl| PDB=2etl | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)''' | '''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)''' | ||
| Line 37: | Line 34: | ||
[[Category: Ray, S S.]] | [[Category: Ray, S S.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
| - | [[Category: | + | [[Category: Deubiquitinating thiol hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:06:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:06, 4 May 2008
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 Page seeded by OCA on Sun May 4 03:06:08 2008
