2kpe: Difference between revisions

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[[Image:2kpe.png|left|200px]]


{{STRUCTURE_2kpe|  PDB=2kpe  |  SCENE=  }}
==Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles==
 
<StructureSection load='2kpe' size='340' side='right'caption='[[2kpe]]' scene=''>
===Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_22649687}}
</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>
==About this Structure==
</table>
[[2kpe]] is a 2 chain structure with sequence 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].  
== 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>
==Reference==
== References ==
<ref group="xtra">PMID:022649687</ref><references group="xtra"/>
<references/>
__TOC__
</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]]

Latest revision as of 09:47, 1 May 2024

Refined structure of Glycophorin A transmembrane segment dimer in DPC micellesRefined structure of Glycophorin A transmembrane segment dimer in DPC micelles

Structural highlights

2kpe is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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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