1kv3

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{{STRUCTURE_1kv3| PDB=1kv3 | SCENE= }}
{{STRUCTURE_1kv3| PDB=1kv3 | SCENE= }}
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'''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM'''
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===HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM===
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==Overview==
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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+.
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(as it appears on PubMed at http://www.pubmed.gov), where 11867708 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11867708}}
==About this Structure==
==About this Structure==
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[[Category: Gtp binding protein]]
[[Category: Gtp binding protein]]
[[Category: Tissue transglutaminase]]
[[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 Wed Jul 2 11:03:45 2008''

Revision as of 08:03, 2 July 2008

Image:1kv3.png

Template:STRUCTURE 1kv3

HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM

Template:ABSTRACT PUBMED 11867708

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

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