1wd9

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[[Image:1wd9.gif|left|200px]]
[[Image:1wd9.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1wd9 |SIZE=350|CAPTION= <scene name='initialview01'>1wd9</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1wd9", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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-arginine_deiminase Protein-arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1wd9| PDB=1wd9 | SCENE= }}
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|RELATEDENTRY=[[1wd8|1WD8]], [[1wda|1WDA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wd9 OCA], [http://www.ebi.ac.uk/pdbsum/1wd9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wd9 RCSB]</span>
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}}
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'''Calcium bound form of human peptidylarginine deiminase type4 (PAD4)'''
'''Calcium bound form of human peptidylarginine deiminase type4 (PAD4)'''
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[[Category: Shimizu, T.]]
[[Category: Shimizu, T.]]
[[Category: Yamada, M.]]
[[Category: Yamada, M.]]
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[[Category: post-translational enzyme]]
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[[Category: Post-translational enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:29:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:45 2008''
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Revision as of 10:29, 3 May 2008

Image:1wd9.gif

Template:STRUCTURE 1wd9

Calcium bound form of human peptidylarginine deiminase type4 (PAD4)


Overview

Peptidylarginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. Its gene is a susceptibility locus for rheumatoid arthritis. Here we present the crystal structure of Ca(2+)-free wild-type PAD4, which shows that the polypeptide chain adopts an elongated fold in which the N-terminal domain forms two immunoglobulin-like subdomains, and the C-terminal domain forms an alpha/beta propeller structure. Five Ca(2+)-binding sites, none of which adopt an EF-hand motif, were identified in the structure of a Ca(2+)-bound inactive mutant with and without bound substrate. These structural data indicate that Ca(2+) binding induces conformational changes that generate the active site cleft. Our findings identify a novel mechanism for enzyme activation by Ca(2+) ions, and are important for understanding the mechanism of protein citrullination and for developing PAD-inhibiting drugs for the treatment of rheumatoid arthritis.

About this Structure

1WD9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for Ca(2+)-induced activation of human PAD4., Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M, Nat Struct Mol Biol. 2004 Aug;11(8):777-83. Epub 2004 Jul 11. PMID:15247907 Page seeded by OCA on Sat May 3 13:29:53 2008

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