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| | ==Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles== | | ==Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles== |
| - | <StructureSection load='2kpe' size='340' side='right'caption='[[2kpe]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kpe' size='340' side='right'caption='[[2kpe]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kpe]] 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=2KPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KPE FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kpf|2kpf]]</div></td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYPA, GPA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> | + | |
| | </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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arseniev, A S]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Bocharov, E V]] | + | [[Category: Bocharov EV]] |
| - | [[Category: Efremov, R G]] | + | [[Category: Efremov RG]] |
| - | [[Category: Goncharuk, M V]] | + | [[Category: Goncharuk MV]] |
| - | [[Category: Mineev, K S]] | + | [[Category: Mineev KS]] |
| - | [[Category: Volynsky, P E]] | + | [[Category: Volynsky PE]] |
| - | [[Category: Blood group antigen]]
| + | |
| - | [[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]]
| + | |
| 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]
Publication Abstract from PubMed
Specific interactions between transmembrane alpha-helices, to a large extent, determine the biological function of integral membrane proteins upon normal development and in pathological states of an organism. Various membrane-like media, partially those mimicking the conditions of multicomponent biological membranes, are used to study the structural and thermodynamic features that define the character of oligomerization of transmembrane helical segments. The choice of the composition of the membrane-mimicking medium is conducted in an effort to obtain a biologically relevant conformation of the protein complex and a sample that would be stable enough to allow to perform a series of long-term experiments with its use. In the present work, heteronuclear NMR spectroscopy and molecular dynamics simulations were used to demonstrate that the two most widely used media (detergent DPC micelles and lipid DMPC/DHPC bicelles) enable to perform structural studies of the specific interactions between transmembrane alpha-helices by the example of dimerizing the transmembrane domain of the bitopic protein glycophorin A. However, a number of peculiarities place lipid bicelles closer to natural lipid bilayers in terms of their physical properties.
Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments.,Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, Arseniev AS Acta Naturae. 2011 Apr;3(2):90-8. PMID:22649687[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
- ↑ Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, Arseniev AS. Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments. Acta Naturae. 2011 Apr;3(2):90-8. PMID:22649687
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