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1kv3

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[[Image:1kv3.gif|left|200px]]
[[Image:1kv3.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1kv3 |SIZE=350|CAPTION= <scene name='initialview01'>1kv3</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1kv3", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= TGM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1kv3| PDB=1kv3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kv3 OCA], [http://www.ebi.ac.uk/pdbsum/1kv3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kv3 RCSB]</span>
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'''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM'''
'''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM'''
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[[Category: Clardy, J.]]
[[Category: Clardy, J.]]
[[Category: Liu, S.]]
[[Category: Liu, S.]]
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[[Category: crystallography]]
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[[Category: Crystallography]]
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[[Category: gtp binding protein]]
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[[Category: Gtp binding protein]]
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[[Category: tissue transglutaminase]]
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[[Category: Tissue transglutaminase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:12:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:56 2008''
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Revision as of 20:12, 2 May 2008

Template:STRUCTURE 1kv3

HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM


Overview

Tissue transglutaminase (TG) is a Ca2+-dependent acyltransferase with roles in cellular differentiation, apoptosis, and other biological functions. In addition to being a transamidase, TG undergoes a GTP-binding/GTPase cycle even though it lacks any obvious sequence similarity with canonical GTP-binding (G) proteins. Guanine nucleotide binding and Ca2+ concentration reciprocally regulate TG's transamidation activity, with nucleotide binding being the negative regulator. Here we report the x-ray structure determined to 2.8-A resolution of human TG complexed with GDP. Although the transamidation active site is similar to those of other known transglutaminases, the guanine nucleotide-binding site of TG differs markedly from other G proteins. The structure suggests a structural basis for the negative regulation of transamidation activity by bound nucleotide, and the positive regulation of transamidation by Ca2+.

About this Structure

1KV3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity., Liu S, Cerione RA, Clardy J, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. Epub 2002 Feb 26. PMID:11867708 Page seeded by OCA on Fri May 2 23:12:09 2008

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