1lyw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1lyw.jpg|left|200px]]
[[Image:1lyw.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1lyw |SIZE=350|CAPTION= <scene name='initialview01'>1lyw</scene>, resolution 2.5&Aring;
+
The line below this paragraph, containing "STRUCTURE_1lyw", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_D Cathepsin D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.5 3.4.23.5] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1lyw| PDB=1lyw | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyw OCA], [http://www.ebi.ac.uk/pdbsum/1lyw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lyw RCSB]</span>
+
-
}}
+
'''CATHEPSIN D AT PH 7.5'''
'''CATHEPSIN D AT PH 7.5'''
Line 29: Line 26:
[[Category: Gulnik, S V.]]
[[Category: Gulnik, S V.]]
[[Category: Lee, A Y.]]
[[Category: Lee, A Y.]]
-
[[Category: aspartic protease]]
+
[[Category: Aspartic protease]]
-
[[Category: glycoprotein]]
+
[[Category: Glycoprotein]]
-
[[Category: hydrolase]]
+
[[Category: Hydrolase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:26:05 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:09:05 2008''
+

Revision as of 21:26, 2 May 2008

Image:1lyw.jpg

Template:STRUCTURE 1lyw

CATHEPSIN D AT PH 7.5


Overview

The crystal structure of a catalytically inactive form of cathepsin D (CatDhi) has been obtained at pH 7.5. The N-terminal strand relocates by 30 A from its position in the interdomain beta-sheet and inserts into the active site cleft, effectively blocking substrate access. CatDhi has a five-stranded interdomain beta-sheet and resembles Intermediate 3, a hypothetical structure proposed to be transiently formed during proteolytic activation of the proenzyme precursor. Interconversion between active and inactive forms of CatD is reversible and may be regulated by an ionizable switch involving the carboxylate side chains of Glu 5, Glu 180, and Asp 187. Our findings provide a structural basis for the pH-dependent regulation of aspartic proteinase activity and suggest a novel mechanism for pH-dependent modulation of substrate specificity.

About this Structure

1LYW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational switching in an aspartic proteinase., Lee AY, Gulnik SV, Erickson JW, Nat Struct Biol. 1998 Oct;5(10):866-71. PMID:9783744 Page seeded by OCA on Sat May 3 00:26:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lyw"
Personal tools