3hx4

<table><tr><td colspan='2'>[[3hx4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HX4 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGME49_101440, CDPK1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5811 TOXGO])</td></tr>

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== Publication Abstract from PubMed ==

Calcium-dependent protein kinases (CDPKs) have pivotal roles in the calcium-signaling pathway in plants, ciliates and apicomplexan parasites and comprise a calmodulin-dependent kinase (CaMK)-like kinase domain regulated by a calcium-binding domain in the C terminus. To understand this intramolecular mechanism of activation, we solved the structures of the autoinhibited (apo) and activated (calcium-bound) conformations of CDPKs from the apicomplexan parasites Toxoplasma gondii and Cryptosporidium parvum. In the apo form, the C-terminal CDPK activation domain (CAD) resembles a calmodulin protein with an unexpected long helix in the N terminus that inhibits the kinase domain in the same manner as CaMKII. Calcium binding triggers the reorganization of the CAD into a highly intricate fold, leading to its relocation around the base of the kinase domain to a site remote from the substrate binding site. This large conformational change constitutes a distinct mechanism in calcium signal-transduction pathways.

Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.,Wernimont AK, Artz JD, Finerty P Jr, Lin YH, Amani M, Allali-Hassani A, Senisterra G, Vedadi M, Tempel W, Mackenzie F, Chau I, Lourido S, Sibley LD, Hui R Nat Struct Mol Biol. 2010 May;17(5):596-601. Epub 2010 May 2. PMID:20436473<ref>PMID:20436473</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3hx4" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Toxgo]]

[[Category: Arrowsmith, C H]]

[[Category: Artz, J D]]

[[Category: Bochkarev, A]]

[[Category: Bountra, C]]

[[Category: Edwards, A M]]

[[Category: Finnerty, P]]

[[Category: Hassani, A A]]

[[Category: He, H]]

[[Category: Hui, R]]

[[Category: Lin, Y H]]

[[Category: Lourido, S]]

[[Category: MacKenzie, F]]

[[Category: Structural genomic]]

[[Category: Sibley, D L]]

[[Category: Sinestera, G]]

[[Category: Vedadi, M]]

[[Category: Wasney, G]]

[[Category: Weigelt, J]]

[[Category: Wernimont, A K]]

[[Category: Xiao, T]]

[[Category: Transferase]]