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
(New page: 200px<br /> <applet load="2etl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2etl, resolution 2.400Å" /> '''Crystal Structure ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2etl.gif|left|200px]]<br /> | + | [[Image:2etl.gif|left|200px]]<br /><applet load="2etl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2etl" size=" | + | |
caption="2etl, resolution 2.400Å" /> | caption="2etl, resolution 2.400Å" /> | ||
'''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)'''<br /> | '''Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ubiquitin C-terminal hydrolase UCH-L1 (PGP9.5) comprises >1% of total | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 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 CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Das, C.]] | [[Category: Das, C.]] | ||
| - | [[Category: Hoang, Q | + | [[Category: Hoang, Q Q.]] |
| - | [[Category: Kreinbring, C | + | [[Category: Kreinbring, C A.]] |
| - | [[Category: Lansbury, P | + | [[Category: Lansbury, P T.]] |
| - | [[Category: Luchansky, S | + | [[Category: Luchansky, S J.]] |
| - | [[Category: Meray, R | + | [[Category: Meray, R K.]] |
| - | [[Category: Petsko, G | + | [[Category: Petsko, G A.]] |
| - | [[Category: Ray, S | + | [[Category: Ray, S S.]] |
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: deubiquitinating thiol hydrolase]] | [[Category: deubiquitinating thiol hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:29 2008'' |
Revision as of 15:14, 21 February 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 with as ligand. 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 Thu Feb 21 17:14:29 2008
