2zht: Difference between revisions

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~~'''~~Crystal structure of BACE1 at pH 4.5~~'''~~

===Crystal structure of BACE1 at pH 4.5===

~~==Overview==~~

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~~BACE1 (beta~~-~~secretase) is a transmembrane aspartic protease that cleaves the beta~~-~~amyloid precursor protein (APP) and generates the amyloid beta peptide (Abeta). BACE1 cycles between the cell surface and the endosomal system many times~~, ~~and becomes activated interconvertibly during its cellular trafficking~~, ~~leading~~ to the ~~production of Abeta~~. ~~Here we report the crystal structure of the catalytically active form of BACE1~~. The active form has novel structural features involving the conformation of the flap and subsites that promote substrate binding. The functionally essential residues and water molecules are well defined, ~~playing a key role in~~ the ~~iterative activation of BACE1~~. ~~Furthermore, we describe the crystal structure of the dehydrated form of BACE1, showing that BACE1 activity is dependent on the dynamics of a catalytically required Asp~~-bound water molecule, which directly affects its catalytic properties. These findings provide insight into a novel regulation of BACE1 activity and elucidate how BACE1 modulates its activity during cellular trafficking.

The line below this paragraph, {{ABSTRACT_PUBMED_18378702}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18378702 is the PubMed ID number.

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==About this Structure==

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[[Category: Transmembrane]]

[[Category: Zymogen]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Apr 24 09~~:46:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:05:04 2008''

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-[[Image:2zht.jpg|left|200px]]
+{{Seed}}
+[[Image:2zht.png|left|200px]]
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 {{STRUCTURE_2zht|  PDB=2zht  |  SCENE=  }}
-'''Crystal structure of BACE1 at pH 4.5'''
+===Crystal structure of BACE1 at pH 4.5===
-==Overview==
+<!--
-BACE1 (beta-secretase) is a transmembrane aspartic protease that cleaves the beta-amyloid precursor protein (APP) and generates the amyloid beta peptide (Abeta). BACE1 cycles between the cell surface and the endosomal system many times, and becomes activated interconvertibly during its cellular trafficking, leading to the production of Abeta. Here we report the crystal structure of the catalytically active form of BACE1. The active form has novel structural features involving the conformation of the flap and subsites that promote substrate binding. The functionally essential residues and water molecules are well defined, playing a key role in the iterative activation of BACE1. Furthermore, we describe the crystal structure of the dehydrated form of BACE1, showing that BACE1 activity is dependent on the dynamics of a catalytically required Asp-bound water molecule, which directly affects its catalytic properties. These findings provide insight into a novel regulation of BACE1 activity and elucidate how BACE1 modulates its activity during cellular trafficking.
+The line below this paragraph, {{ABSTRACT_PUBMED_18378702}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18378702 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18378702}}
 ==About this Structure==
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 [[Category: Transmembrane]]
 [[Category: Zymogen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:46:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:05:04 2008''