1ef7: Difference between revisions

Revision as of 00:36, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ef7.png

Template:STRUCTURE 1ef7

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN XCRYSTAL STRUCTURE OF HUMAN CATHEPSIN X

Template:ABSTRACT PUBMED 10745011

About this StructureAbout this Structure

1EF7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease., Guncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L, Turk D, Structure. 2000 Mar 15;8(3):305-13. PMID:10745011

Page seeded by OCA on Tue Jul 1 00:36:19 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ef7.jpg|left|200px]]
+{{Seed}}
+[[Image:1ef7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ef7|  PDB=1ef7  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X'''
+===CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X===
-==Overview==
+<!--
-BACKGROUND: Cathepsin X is a widespread, abundantly expressed papain-like mammalian lysosomal cysteine protease. It exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity and shares a similar activity profile with cathepsin B. The latter has been implicated in normal physiological events as well as in various pathological states such as rheumatoid arthritis, Alzheimer's disease and cancer progression. Thus the question is raised as to which of the two enzyme activities has actually been monitored. RESULTS: The crystal structure of human cathepsin X has been determined at 2.67 A resolution. The structure shares the common features of a papain-like enzyme fold, but with a unique active site. The most pronounced feature of the cathepsin X structure is the mini-loop that includes a short three-residue insertion protruding into the active site of the protease. The residue Tyr27 on one side of the loop forms the surface of the S1 substrate-binding site, and His23 on the other side modulates both carboxy-monopeptidase as well as carboxy-dipeptidase activity of the enzyme by binding the C-terminal carboxyl group of a substrate in two different sidechain conformations. CONCLUSIONS: The structure of cathepsin X exhibits a binding surface that will assist in the design of specific inhibitors of cathepsin X as well as of cathepsin B and thereby help to clarify the physiological roles of both proteases.
+The line below this paragraph, {{ABSTRACT_PUBMED_10745011}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10745011 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10745011}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Cysteine protease]]
 [[Category: Papain-like]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:01:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:36:19 2008''