2htg
From Proteopedia
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| - | [[Image:2htg.gif|left|200px]] | + | [[Image:2htg.gif|left|200px]] |
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| - | '''Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger''' | + | {{Structure |
| + | |PDB= 2htg |SIZE=350|CAPTION= <scene name='initialview01'>2htg</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HTG is a [ | + | 2HTG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTG OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional characterization of transmembrane segment VII of the Na+/H+ exchanger isoform 1., Ding J, Rainey JK, Xu C, Sykes BD, Fliegel L, J Biol Chem. 2006 Oct 6;281(40):29817-29. Epub 2006 Jul 21. PMID:[http:// | + | Structural and functional characterization of transmembrane segment VII of the Na+/H+ exchanger isoform 1., Ding J, Rainey JK, Xu C, Sykes BD, Fliegel L, J Biol Chem. 2006 Oct 6;281(40):29817-29. Epub 2006 Jul 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16861220 16861220] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ding, J.]] | [[Category: Ding, J.]] | ||
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[[Category: transmembrane segment]] | [[Category: transmembrane segment]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:21:21 2008'' |
Revision as of 15:21, 20 March 2008
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Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger
Overview
The Na(+)/H(+) exchanger isoform 1 is an integral membrane protein that regulates intracellular pH by exchanging one intracellular H(+) for one extracellular Na(+). It is composed of an N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain. We characterized the structural and functional aspects of the critical transmembrane segment VII (TM VII, residues 251-273) by using alanine scanning mutagenesis and high resolution NMR. Each residue of TM VII was mutated to alanine, the full-length protein expressed, and its activity characterized. TM VII was sensitive to mutation. Mutations at 13 of 22 residues resulted in severely reduced activity, whereas other mutants exhibited varying degrees of decreases in activity. The impaired activities sometimes resulted from low expression and/or low surface targeting. Three of the alanine scanning mutant proteins displayed increased, and two displayed decreased resistance to the Na(+)/H(+) exchanger isoform 1 inhibitor EMD87580. The structure of a peptide of TM VII was determined by using high resolution NMR in dodecylphosphocholine micelles. TM VII is predominantly alpha-helical, with a break in the helix at the functionally critical residues Gly(261)-Glu(262). The relative positions and orientations of the N- and C-terminal helical segments are seen to vary about this extended segment in the ensemble of NMR structures. Our results show that TM VII is a critical transmembrane segment structured as an interrupted helix, with several residues that are essential to both protein function and sensitivity to inhibition.
About this Structure
2HTG is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of transmembrane segment VII of the Na+/H+ exchanger isoform 1., Ding J, Rainey JK, Xu C, Sykes BD, Fliegel L, J Biol Chem. 2006 Oct 6;281(40):29817-29. Epub 2006 Jul 21. PMID:16861220
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