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| | ==DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES== | | ==DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES== |
| - | <StructureSection load='1afo' size='340' side='right'caption='[[1afo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1afo' size='340' side='right'caption='[[1afo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1afo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1afo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFO FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afo OCA], [https://pdbe.org/1afo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afo RCSB], [https://www.ebi.ac.uk/pdbsum/1afo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afo ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afo OCA], [https://pdbe.org/1afo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afo RCSB], [https://www.ebi.ac.uk/pdbsum/1afo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLPA_HUMAN GLPA_HUMAN]] Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).<ref>PMID:8009226</ref> <ref>PMID:10926825</ref> <ref>PMID:12813056</ref> <ref>PMID:14604989</ref> <ref>PMID:15331714</ref> <ref>PMID:19438409</ref>
| + | [https://www.uniprot.org/uniprot/GLPA_HUMAN GLPA_HUMAN] Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).<ref>PMID:8009226</ref> <ref>PMID:10926825</ref> <ref>PMID:12813056</ref> <ref>PMID:14604989</ref> <ref>PMID:15331714</ref> <ref>PMID:19438409</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Engelman, D M]] | + | [[Category: Engelman DM]] |
| - | [[Category: Mackenzie, K R]] | + | [[Category: Mackenzie KR]] |
| - | [[Category: Prestegard, J H]] | + | [[Category: Prestegard JH]] |
| - | [[Category: Human glycophorin some]]
| + | |
| - | [[Category: Integral membrane protein]]
| + | |
| - | [[Category: Membrane protein folding]]
| + | |
| - | [[Category: Transmembrane helix interaction]]
| + | |
| Structural highlights
Function
GLPA_HUMAN Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV).[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning alpha helices cross at an angle of -40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.
A transmembrane helix dimer: structure and implications.,MacKenzie KR, Prestegard JH, Engelman DM Science. 1997 Apr 4;276(5309):131-3. PMID:9082985[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sim BK, Chitnis CE, Wasniowska K, Hadley TJ, Miller LH. Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science. 1994 Jun 24;264(5167):1941-4. PMID:8009226
- ↑ Young MT, Beckmann R, Toye AM, Tanner MJ. Red-cell glycophorin A-band 3 interactions associated with the movement of band 3 to the cell surface. Biochem J. 2000 Aug 15;350 Pt 1:53-60. PMID:10926825
- ↑ Young MT, Tanner MJ. Distinct regions of human glycophorin A enhance human red cell anion exchanger (band 3; AE1) transport function and surface trafficking. J Biol Chem. 2003 Aug 29;278(35):32954-61. Epub 2003 Jun 17. PMID:12813056 doi:http://dx.doi.org/10.1074/jbc.M302527200
- ↑ Bruce LJ, Pan RJ, Cope DL, Uchikawa M, Gunn RB, Cherry RJ, Tanner MJ. Altered structure and anion transport properties of band 3 (AE1, SLC4A1) in human red cells lacking glycophorin A. J Biol Chem. 2004 Jan 23;279(4):2414-20. Epub 2003 Nov 5. PMID:14604989 doi:http://dx.doi.org/10.1074/jbc.M309826200
- ↑ Sanchez G, Aragones L, Costafreda MI, Ribes E, Bosch A, Pinto RM. Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane. J Virol. 2004 Sep;78(18):9807-13. PMID:15331714 doi:http://dx.doi.org/10.1128/JVI.78.18.9807-9813.2004
- ↑ Pang AJ, Reithmeier RA. Interaction of anion exchanger 1 and glycophorin A in human erythroleukaemic K562 cells. Biochem J. 2009 Jul 15;421(3):345-56. doi: 10.1042/BJ20090345. PMID:19438409 doi:http://dx.doi.org/10.1042/BJ20090345
- ↑ MacKenzie KR, Prestegard JH, Engelman DM. A transmembrane helix dimer: structure and implications. Science. 1997 Apr 4;276(5309):131-3. PMID:9082985
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