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2ygg

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Revision as of 00:39, 5 August 2016

Complex of CaMBR and CaM

Structural highlights

2ygg is a 2 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1y4e, 2bec, 3cln, 1qx5, 1qx7, 1g4y, 1niw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lin X, Barber DL. A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12631-6. PMID:8901634
↑ Pang T, Su X, Wakabayashi S, Shigekawa M. Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers. J Biol Chem. 2001 May 18;276(20):17367-72. Epub 2001 Feb 28. PMID:11350981 doi:http://dx.doi.org/10.1074/jbc.M100296200
↑ Pang T, Hisamitsu T, Mori H, Shigekawa M, Wakabayashi S. Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements. Biochemistry. 2004 Mar 30;43(12):3628-36. PMID:15035633 doi:http://dx.doi.org/10.1021/bi0360004
↑ Koester S, Pavkov-Keller T, Kuehlbrandt W, Yildiz O. Structure of human Na+/H+ exchanger NHE1 regulatory region in complex with CaM and Ca2+ J Biol Chem. 2011 Sep 19. PMID:21931166 doi:10.1074/jbc.M111.286906

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ygg"

Categories: Buffalo rat | Human | Koester, S | Yildiz, O | Metal binding protein-transport protein complex

@@ Line 1: / Line 1: @@
 ==Complex of CaMBR and CaM==
 <StructureSection load='2ygg' size='340' side='right' caption='[[2ygg]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
+<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://pdbe.org/2ygg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ygg RCSB], [http://www.ebi.ac.uk/pdbsum/2ygg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ygg" style="background-color:#fffaf0;"></div>
 ==See Also==

2ygg

From Proteopedia

Revision as of 00:39, 5 August 2016

Complex of CaMBR and CaM

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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