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| - | {{Seed}} | |
| - | [[Image:2kpe.jpg|left|200px]] | |
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| - | <!--
| + | ==Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles== |
| - | The line below this paragraph, containing "STRUCTURE_2kpe", creates the "Structure Box" on the page.
| + | <StructureSection load='2kpe' size='340' side='right'caption='[[2kpe]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2kpe]] 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=2KPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KPE FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </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=2kpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kpe OCA], [https://pdbe.org/2kpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kpe RCSB], [https://www.ebi.ac.uk/pdbsum/2kpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kpe ProSAT]</span></td></tr> |
| - | {{STRUCTURE_2kpe| PDB=2kpe | SCENE= }}
| + | </table> |
| - | | + | == Function == |
| - | ===Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles===
| + | [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> |
| - | | + | == References == |
| - | | + | <references/> |
| - | ==About this Structure== | + | __TOC__ |
| - | 2KPE is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KPE OCA].
| + | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Arseniev, A S.]] | + | [[Category: Large Structures]] |
| - | [[Category: Bocharov, E V.]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Efremov, R G.]] | + | [[Category: Bocharov EV]] |
| - | [[Category: Goncharuk, M V.]] | + | [[Category: Efremov RG]] |
| - | [[Category: Mineev, K S.]] | + | [[Category: Goncharuk MV]] |
| - | [[Category: Volynsky, P E.]] | + | [[Category: Mineev KS]] |
| - | [[Category: Blood group antigen]] | + | [[Category: Volynsky PE]] |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Glycophorin some]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Host-virus interaction]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Micelle]]
| + | |
| - | [[Category: Sialic acid]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transmembrane dimer]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:41:18 2010''
| + | |
| 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]
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
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