1bts: Difference between revisions

Revision as of 11:56, 2 May 2008

THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3

OverviewOverview

We have studied the structures of synthetic peptides which correspond to the proposed first and second membrane-spanning segments of the human red cell anion transporter (band 3). The peptides, which were acetylated at their N-termini and amidated at the C-termini, comprise the 20 amino acids of residues 405-424 and 21 amino acids of residues 436-456 of the human band 3 sequence. The solution structures of the peptides in trifluoroethanol were studied by two-dimensional NMR spectroscopy. Characteristic NOEs were observed indicating that the peptides adopted a predominantly alpha-helical structure in trifluoroethanol solution. Dynamical simulated annealing using the program XPLOR was employed for the structure calculations. The amide exchange rates in trifluoroethanol have also been measured and are consistent with an alpha-helical structure for the peptides.

About this StructureAbout this Structure

1BTS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The solution structures of the first and second transmembrane-spanning segments of band 3., Gargaro AR, Bloomberg GB, Dempsey CE, Murray M, Tanner MJ, Eur J Biochem. 1994 Apr 1;221(1):445-54. PMID:8168533 Page seeded by OCA on Fri May 2 11:56:51 2008

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OCA

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 [[Image:1bts.gif|left|200px]]
- {{Structure
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-}}
 '''THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3'''
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 [[Category: Murray, M.]]
 [[Category: Tanner, M J.A.]]
-[[Category: transmembrane protein]]
+[[Category: Transmembrane protein]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:56:51 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:16 2008''