1ito: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ito.jpg|left|200px]] | [[Image:1ito.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1ito", 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_1ito| PDB=1ito | SCENE= }} | |||
}} | |||
'''Crystal Structure Analysis of Bovine Spleen Cathepsin B-E64c complex''' | '''Crystal Structure Analysis of Bovine Spleen Cathepsin B-E64c complex''' | ||
| Line 34: | Line 31: | ||
[[Category: Tomoo, T.]] | [[Category: Tomoo, T.]] | ||
[[Category: Yamamoto, A.]] | [[Category: Yamamoto, A.]] | ||
[[Category: | [[Category: Cathepsin b]] | ||
[[Category: | [[Category: Cysteine protease]] | ||
[[Category: | [[Category: E64c]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:24:00 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:24, 2 May 2008
Crystal Structure Analysis of Bovine Spleen Cathepsin B-E64c complex
Overview
In order to elucidate the substrate specificity of the Sn subsites (n=1-3) of cathepsin B, its crystal structure inhibited by E64c [(+)-(2S,3S)-3-(1-[N-(3-methylbutyl)amino]-leucylcarbonyl)oxirane-2-carbox ylic acid] was analyzed by the X-ray diffraction method. Iterative manual rebuilding and convenient conjugate refinement of structure decreased R- and free R-factors to 19.7% and to 23.9%, respectively, where 130 water molecules were included for the refinement using 14,759 independent reflections from 10 to 2.3 A resolution. The epoxy carbonyl carbon of E64c was covalently bonded to the Cys(29) S(gamma) atom and the remaining parts were located at Sn subsites (n=1-3). The substrate specificity of these subsites was characterized based on their interactions with the inhibitor. Base on these structural data, we developed a novel cathepsin B-specific noncovalent-type inhibitor, which may bind to S2'-S3. The molecular design of possessing structural elements of both CA074 and E64c, assisted by energy minimization and molecular dynamics (MD) simulation, may lead to a new lead noncovalent-type inhibitor.
About this Structure
1ITO is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis for development of cathepsin B-specific noncovalent-type inhibitor: crystal structure of cathepsin B-E64c complex., Yamamoto A, Tomoo K, Matsugi K, Hara T, In Y, Murata M, Kitamura K, Ishida T, Biochim Biophys Acta. 2002 Jun 3;1597(2):244-51. PMID:12044902 Page seeded by OCA on Fri May 2 20:24:00 2008
