2ygg | pdb_00002ygg

COMPLEX OF CAMBR AND CAM

spinqualitylabelsall models 2ygg, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ygg is a 2 chain structure with sequence from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MPD, MRD, TAM Related: 1y4e, 2bec, 3cln, 1qx5, 1qx7, 1g4y, 1niw Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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