4upu: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4upu" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==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]] | |||
