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2htg

From Proteopedia

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[[Image:2htg.gif|left|200px]]
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{{STRUCTURE_2htg| PDB=2htg | SCENE= }}
{{STRUCTURE_2htg| PDB=2htg | SCENE= }}
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'''Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger'''
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===Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16861220 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16861220}}
==About this Structure==
==About this Structure==
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2HTG is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTG OCA].
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2HTG is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTG OCA].
==Reference==
==Reference==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Transmembrane segment]]
[[Category: Transmembrane segment]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:41:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:11:08 2008''

Revision as of 04:11, 29 July 2008

Image:2htg.png

Template:STRUCTURE 2htg

Structural and functional characterization of TM VII of the NHE1 isoform of the Na+/H+ exchanger

Template:ABSTRACT PUBMED 16861220

About this Structure

2HTG is a Single protein structure. Full experimental 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

Page seeded by OCA on Tue Jul 29 07:11:08 2008

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