6bjf

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==NMR Structural and biophysical functional analysis of intracellular loop 5 of the NHE1 isoform of the Na+/H+ exchanger.==
==NMR Structural and biophysical functional analysis of intracellular loop 5 of the NHE1 isoform of the Na+/H+ exchanger.==
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<StructureSection load='6bjf' size='340' side='right'caption='[[6bjf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6bjf' size='340' side='right'caption='[[6bjf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6bjf]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BJF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6bjf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BJF FirstGlance]. <br>
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</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=6bjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bjf OCA], [http://pdbe.org/6bjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bjf RCSB], [http://www.ebi.ac.uk/pdbsum/6bjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bjf ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bjf OCA], [https://pdbe.org/6bjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bjf RCSB], [https://www.ebi.ac.uk/pdbsum/6bjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bjf ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SL9A1_HUMAN SL9A1_HUMAN] Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.<ref>PMID:8901634</ref> <ref>PMID:11350981</ref> <ref>PMID:15035633</ref>
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The mammalian Na(+)/H(+) exchanger isoform 1 (NHE1) is an integral membrane protein that regulates intracellular pH (pHi) by removing a single intracellular proton in exchange for one extracellular sodium ion. It is involved in cardiac hypertrophy and ischemia reperfusion damage to the heart and elevation of its activity is a trigger for breast cancer metastasis. NHE1 has an extensive 500 amino acid N-terminal membrane domain that mediates transport and consists of 12 transmembrane segments connected by intracellular and extracellular loops. Intracellular loops are hypothesized to modulate the sensitivity to pHi. In this study, we characterized the structure and function of intracellular loop 5 (IL5), specifically amino acids 431-443. Mutation of eleven residues to alanine caused partial or nearly complete inhibition of transport; notably, mutation of residues L432, T433, I436, N437, R440 and K443 demonstrated these residues had critical roles in NHE1 function independent of effects on targeting or expression. The nuclear magnetic resonance (NMR) solution spectra of the IL5 peptide in a membrane mimetic sodium dodecyl sulfate solution revealed that IL5 has a stable three-dimensional structure with substantial alpha helical character. NMR chemical shifts indicated that K438 was in close proximity with W434. Overall, our results show that IL5 is a critical, intracellular loop with a propensity to form an alpha helix, and many residues of this intracellular loop are critical to proton sensing and ion transport.
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Diverse residues of intracellular loop 5 of the Na(+)/H(+) exchanger modulate proton sensing, expression, activity and targeting.,Wong KY, McKay R, Liu Y, Towle K, Elloumi Y, Li X, Quan S, Dutta D, Sykes BD, Fliegel L Biochim Biophys Acta Biomembr. 2019 Jan;1861(1):191-200. doi:, 10.1016/j.bbamem.2018.07.014. Epub 2018 Jul 31. PMID:30071192<ref>PMID:30071192</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6bjf" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fliegel, L]]
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[[Category: Fliegel L]]
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[[Category: McKay, R]]
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[[Category: McKay R]]
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[[Category: Towle, K]]
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[[Category: Towle K]]
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[[Category: Wong, K]]
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[[Category: Wong K]]
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[[Category: Membrane protein]]
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[[Category: Structure from cyana 2 1]]
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Current revision

NMR Structural and biophysical functional analysis of intracellular loop 5 of the NHE1 isoform of the Na+/H+ exchanger.

PDB ID 6bjf

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