4upu
From Proteopedia
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| - | ''' | + | ==Crystal structure of calmodulin== |
| + | <StructureSection load='4upu' size='340' side='right' caption='[[4upu]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4upu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UPU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UPU FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-trisphosphate_3-kinase Inositol-trisphosphate 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.127 2.7.1.127] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4upu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4upu RCSB], [http://www.ebi.ac.uk/pdbsum/4upu PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Inositol 1,4,5-triphoshate 3-kinase (IP3 3-K) is a key enzyme that catalyses the synthesis of inositol 1,3,4,5-tetrakisphosphate (IP4), using IP3 and ATP as substrates. Both inositides, substrate and product, present crucial roles in the cell. IP3 is a key point in Ca2+ metabolism that promotes Ca2+ release from intracellular stores and together with IP4 regulates Ca2+ homeostasis. In addition, IP4 is involved in the immune cell development. It has been proved that Ca2+/calmodulin (Ca2+/CaM) regulates the activity of IP3 3-K, via direct interaction between both enzymes. Although we have extensive structural knowledge of the kinase domains of the three IP3 3-K isoforms, no structural information is available about the interaction between IP3 3-K and Ca2+/CaM. Here we describe the crystal structure of the complex between human Ca2+/CaM and the CaM binding region of human IP3 3-K isoform A (residues 158 to 183), and propose a model for a complex including the kinase domain. The structure obtained allowed us to identify all the key residues involved in the interaction, which have been evaluated by site directed mutagenesis, pull-down and fluorescence anisotropy experiments. The results allowed the identification of a new CaM binding motif expanding our knowledge about how CaM interacts with its partners. | ||
| - | + | A new calmodulin binding motif for inositol 1,4,5-trisphosphate 3-kinase regulation.,Franco-Echevarria E, Banos-Sanz JI, Monterroso B, Round A, Sanz-Aparicio J, Gonzalez B Biochem J. 2014 Aug 7. PMID:25101901<ref>PMID:25101901</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Inositol-trisphosphate 3-kinase]] | ||
| + | [[Category: Banos-Sanz, J I.]] | ||
| + | [[Category: Franco-Echevarria, E.]] | ||
| + | [[Category: Gonzalez, B.]] | ||
| + | [[Category: Monterroso, B.]] | ||
| + | [[Category: Round, A.]] | ||
| + | [[Category: Sanz-Aparicio, J.]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:20, 20 August 2014
Crystal structure of calmodulin
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