1bts: Difference between revisions
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'''THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3'''<br /> | '''THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3'''<br /> | ||
==Overview== | ==Overview== | ||
We have studied the structures of synthetic peptides which correspond to | 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. | ||
==Disease== | ==Disease== | ||
Known diseases associated with this structure: | Known diseases associated with this structure: Blood group, Diego OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Froese , OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Waldner OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Blood group, Wright OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Diabetes insipidus, nephrogenic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300538 300538]], Hemolytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Malaria, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Nephrogenic syndrome of inappropriate antidiuresis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300538 300538]], Ovalocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Renal tubular acidosis, distal, AD OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Renal tubular acidosis, distal, AR OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]], Spherocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109270 109270]] | ||
==About this Structure== | ==About this Structure== | ||
1BTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1BTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTS OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bloomberg, G | [[Category: Bloomberg, G B.]] | ||
[[Category: Dempsey, C | [[Category: Dempsey, C E.]] | ||
[[Category: Gargaro, A | [[Category: Gargaro, A R.]] | ||
[[Category: Murray, M.]] | [[Category: Murray, M.]] | ||
[[Category: Tanner, M | [[Category: Tanner, M J.A.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: transmembrane protein]] | [[Category: transmembrane protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:02 2008'' | ||
Revision as of 12:59, 21 February 2008
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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.
DiseaseDisease
Known diseases associated with this structure: Blood group, Diego OMIM:[109270], Blood group, Froese , OMIM:[109270], Blood group, Waldner OMIM:[109270], Blood group, Wright OMIM:[109270], Diabetes insipidus, nephrogenic OMIM:[300538], Hemolytic anemia OMIM:[109270], Malaria, resistance to OMIM:[109270], Nephrogenic syndrome of inappropriate antidiuresis OMIM:[300538], Ovalocytosis OMIM:[109270], Renal tubular acidosis, distal, AD OMIM:[109270], Renal tubular acidosis, distal, AR OMIM:[109270], Spherocytosis OMIM:[109270]
About this StructureAbout this Structure
1BTS is a Single protein structure of sequence from Homo sapiens with and 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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