1bts
THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3
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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.
DiseaseDisease
Known diseases associated with this structure: Acanthocytosis, one form OMIM:[109270], Blood group, Diego OMIM:[109270], Blood group, Waldner OMIM:[109270], Blood group, Wright OMIM:[109270], Diabetes insipidus, nephrogenic OMIM:[300538], Elliptocytosis, Malaysian-Melanesian type OMIM:[109270], Hemolytic anemia due to band 3 defect defect OMIM:[109270], Nephrogenic syndrome of inappropriate antidiuresis OMIM:[300538], OMIM:[[1]]109270, Renal tubular acidosis, distal, 179800 OMIM:[109270], Spherocytosis, hereditary OMIM:[109270]
About this StructureAbout this Structure
1BTS is a Single protein structure of sequence from Homo sapiens with ACE and NH2 as ligands. 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
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