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2E30

Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1

Summary for 2E30
Entry DOI10.2210/pdb2e30/pdb
DescriptorCalcium-binding protein p22, Sodium/hydrogen exchanger 1, CALCIUM ION (3 entities in total)
Functional Keywordstransporter, ef-hand, complex structure, metal binding protein-transport protein complex, metal binding protein/transport protein
Biological sourceHomo sapiens (human)
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Cellular locationCytoplasm (By similarity): Q99653
Membrane; Multi-pass membrane protein: P19634
Total number of polymer chains2
Total formula weight27583.04
Authors
Mishima, M.,Wakabayashi, S.,Kojima, C. (deposition date: 2006-11-19, release date: 2006-12-19, Last modification date: 2024-05-29)
Primary citationMishima, M.,Wakabayashi, S.,Kojima, C.
Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1
J.Biol.Chem., 282:2741-2751, 2007
Cited by
PubMed Abstract: Na+/H+ exchanger 1 (NHE1) regulates intracellular pH, Na+ content, and cell volume. Calcineurin B homologous protein 1 (CHP1) serves as an essential cofactor that facilitates NHE1 exchange activity under physiological conditions by direct binding to the cytoplasmic juxtamembrane region of NHE1. Here we describe the solution structure of the cytoplasmic juxtamembrane region of NHE1 complexed with CHP1. The region of NHE1 forms an amphipathic helix, which is induced by CHP1 binding, and CHP1 possesses a large hydrophobic cleft formed by EF-hand helices. The apolar side of the NHE1 helix participates in extensive hydrophobic interactions with the cleft of CHP1. We suggest that helix formation of the cytoplasmic region of NHE1 by CHP1 is a prerequisite for generating the active form of NHE1. The molecular recognition detailed in this study also provides novel insight into the target binding mechanism of EF-hand proteins.
PubMed: 17050540
DOI: 10.1074/jbc.M604092200
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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