3pbh: Difference between revisions

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==Overview==

A wild-type human procathepsin B was expressed, crystallized in two, crystal forms and its crystal structure determined at 3.2 and 3.3, Angstroms resolution. The structure reveals that the propeptide folds on, the cathepsin B surface, shielding the enzyme active site from exposure to, solvent. The structure of the enzymatically active domains is virtually, identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are, lifted above the body of the mature enzyme, supporting the propeptide, structure.

A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.

==About this Structure==

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[[Category: thiol protease]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:42 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-A wild-type human procathepsin B was expressed, crystallized in two, crystal forms and its crystal structure determined at 3.2 and 3.3, Angstroms resolution. The structure reveals that the propeptide folds on, the cathepsin B surface, shielding the enzyme active site from exposure to, solvent. The structure of the enzymatically active domains is virtually, identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are, lifted above the body of the mature enzyme, supporting the propeptide, structure.
+A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.
 ==About this Structure==
@@ Line 25: / Line 25: @@
 [[Category: thiol protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:44:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:42 2008''