2ygg
From Proteopedia
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| - | [[ | + | ==COMPLEX OF CAMBR AND CAM== |
| + | <StructureSection load='2ygg' size='340' side='right' caption='[[2ygg]], [[Resolution|resolution]] 2.23Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ygg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YGG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y4e|1y4e]], [[2bec|2bec]], [[3cln|3cln]], [[1qx5|1qx5]], [[1qx7|1qx7]], [[1g4y|1g4y]], [[1niw|1niw]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ygg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ygg RCSB], [http://www.ebi.ac.uk/pdbsum/2ygg PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ubiquitous mammalian Na(+)/H(+)-exchanger NHE1 has critical functions in regulating intracellular pH, salt concentration and cellular volume. The regulatory C-terminal domain of NHE1 is linked to the ion-translocating N-terminal membrane domain, and acts as a scaffold for signalling complexes. A major interaction partner is calmodulin (CaM), which binds to two neighbouring regions of NHE1 in a strongly Ca(2+) dependent manner. Upon CaM binding, NHE1 is activated by a shift in sensitivity towards alkaline intracellular pH. Here we report the 2.23 A crystal structure of the NHE1 CaM binding region (NHE1(CaMBR)) in complex with CaM and Ca(2+). The C- and N-lobes of CaM bind the first and second helix of NHE1(CaMBR), respectively. Both the NHE1 helices and Ca(2+)-bound CaM are elongated, as confirmed by small angle X-ray scattering analysis. Our X-ray structure sheds new light on the molecular mechanisms of the phosphorylation-dependent regulation of NHE1 and enables us to propose a model of how Ca(2+) regulates NHE1 activity. | ||
| - | + | Structure of human Na+/H+ exchanger NHE1 regulatory region in complex with CaM and Ca2+,Koester S, Pavkov-Keller T, Kuehlbrandt W, Yildiz O J Biol Chem. 2011 Sep 19. PMID:21931166<ref>PMID:21931166</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
Revision as of 11:53, 29 October 2014
COMPLEX OF CAMBR AND CAM
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