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| [[Image:1bzk.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1bzk| PDB=1bzk | SCENE= }} | | {{STRUCTURE_1bzk| PDB=1bzk | SCENE= }} |
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| '''STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.'''
| | ===STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.=== |
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| ==Overview==
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| We have carried out a solution-state NMR study of synthetic peptides patterned on the first membrane span of normal human band 3, and the same region of the mutant band 3 present in Southeast Asian ovalocytosis (SAO) which has a nine amino acid deletion. In 1:1 (v/v) chloroform/methanol, the 42 residue normal peptide (R389-K430) consisted of three helical regions. The slow solvent exchange of backbone amide protons revealed the helix from P403 to A416 was more stable than the "cytoplasmic" N-terminal helix from P391 to A400. These helices were separated by a sharp bend at P403, which is probably located at the boundary between the cytoplasmic domain and the first transmembrane span. The SAO deletion (A400-A408) removed the bend at P403, to leave a stable helix from P391 to A416 containing the residuum of the normal first transmembrane helix and with a hydrophobic turn replaced by a polar turn in the SAO peptide. Insertion of fragments of normal band 3 and band 3 SAO into microsomal membranes was investigated using a cell free translation system. A fragment composed of the cytoplasmic domain and the putative first membrane domain of normal band 3 (B3(1)) inserted stably into the membrane. However, the corresponding fragment of band 3 SAO [SAO(1)] did not integrate stably into membranes. Our results suggest that in SAO band 3, the region of the first membrane span of normal band 3 does not integrate properly into the membrane because it lacks a sufficiently long hydrophobic segment, and the deletion also disrupts a conserved structural subdomain at the membrane surface.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9887277}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9887277 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9887277}} |
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| ==About this Structure== | | ==About this Structure== |
| 1BZK is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZK OCA]. | | 1BZK is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZK OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Synthetic peptide]] | | [[Category: Synthetic peptide]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:09:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:00:03 2008'' |
