1l9m: Difference between revisions

Revision as of 12:02, 2 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:1l9m.png

Template:STRUCTURE 1l9m

Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activationThree-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

Template:ABSTRACT PUBMED 11980702

About this StructureAbout this Structure

1L9M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation., Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM, EMBO J. 2002 May 1;21(9):2055-67. PMID:11980702

Page seeded by OCA on Wed Jul 2 12:02:21 2008

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

OCA

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-'''Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation'''
+===Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation===
-==Overview==
+<!--
-Transglutaminase (TGase) enzymes catalyze the formation of covalent cross-links between protein-bound glutamines and lysines in a calcium-dependent manner, but the role of Ca(2+) ions remains unclear. The TGase 3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. We have solved the three-dimensional structures of the zymogen and the activated forms at 2.2 and 2.1 A resolution, respectively, and examined the role of Ca(2+) ions. The zymogen binds one ion tightly that cannot be exchanged. Upon proteolysis, the enzyme exothermally acquires two more Ca(2+) ions that activate the enzyme, are exchangeable and are functionally replaceable by other lanthanide trivalent cations. Binding of a Ca(2+) ion at one of these sites opens a channel which exposes the key Trp236 and Trp327 residues that control substrate access to the active site. Together, these biochemical and structural data reveal for the first time in a TGase enzyme that Ca(2+) ions induce structural changes which at least in part dictate activity and, moreover, may confer substrate specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11980702}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11980702 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11980702}}
 ==About this Structure==
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 [[Category: Transglutaminase]]
 [[Category: X-ray structure]]
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