5eh4

From Proteopedia

(Difference between revisions)

Revision as of 12:39, 23 December 2015

Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase

Structural highlights

5eh4 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	5eh6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded alpha-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-alpha-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophorin A (GpA) model system, whose homodimeric TM helix interface has been characterized by solution and solid-state NMR and biochemical techniques but never crystallographically. We report that a GpA-TM peptide readily crystallized in a monoolein cubic phase bilayer, yielding a dimeric alpha-helical structure that is in excellent agreement with previously reported NMR measurements made in several different types of host media. These results provide compelling support for the wider application of LCP techniques to enable X-ray crystallographic analysis of single-pass TM interactions.

Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase.,Trenker R, Call ME, Call MJ J Am Chem Soc. 2015 Dec 10. PMID:26642914^[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
↑ Trenker R, Call ME, Call MJ. Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase. J Am Chem Soc. 2015 Dec 10. PMID:26642914 doi:http://dx.doi.org/10.1021/jacs.5b11354

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5eh4"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase==
+<StructureSection load='5eh4' size='340' side='right' caption='[[5eh4]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5eh4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EH4 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eh6|5eh6]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eh4 OCA], [http://pdbe.org/5eh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5eh4 PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://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;">
+== Publication Abstract from PubMed ==
+The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded alpha-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-alpha-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophorin A (GpA) model system, whose homodimeric TM helix interface has been characterized by solution and solid-state NMR and biochemical techniques but never crystallographically. We report that a GpA-TM peptide readily crystallized in a monoolein cubic phase bilayer, yielding a dimeric alpha-helical structure that is in excellent agreement with previously reported NMR measurements made in several different types of host media. These results provide compelling support for the wider application of LCP techniques to enable X-ray crystallographic analysis of single-pass TM interactions.
-The entry 5eh4 is ON HOLD  until Paper Publication
+Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase.,Trenker R, Call ME, Call MJ J Am Chem Soc. 2015 Dec 10. PMID:26642914<ref>PMID:26642914</ref>
-Authors: Call, M.J., Call, M.E., Trenker, R.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+<div class="pdbe-citations 5eh4" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Call, M.E]]
+<references/>
-[[Category: Call, M.J]]
+__TOC__
+</StructureSection>
+[[Category: Call, M E]]
+[[Category: Call, M J]]
 [[Category: Trenker, R]]
+[[Category: Lipidic cubic phase]]
+[[Category: Membrane protein]]
+[[Category: Peptide]]
+[[Category: Receptor]]
+[[Category: Transmembrane]]

5eh4

From Proteopedia

Revision as of 12:39, 23 December 2015

Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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