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==Local refinement of Band 3-III cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex==
==Local refinement of Band 3-III cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex==
<StructureSection load='7v0y' size='340' side='right'caption='[[7v0y]]' scene=''>
<StructureSection load='7v0y' size='340' side='right'caption='[[7v0y]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[7v0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0Y 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=7v0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0y OCA], [https://pdbe.org/7v0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0y RCSB], [https://www.ebi.ac.uk/pdbsum/7v0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0y ProSAT]</span></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=7v0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0y OCA], [https://pdbe.org/7v0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0y RCSB], [https://www.ebi.ac.uk/pdbsum/7v0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0y ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[https://omim.org/entry/109270 109270]]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:1722314</ref> <ref>PMID:1538405</ref>  Defects in SLC4A1 are the cause of spherocytosis type 4 (SPH4) [MIM:[https://omim.org/entry/612653 612653]]; also known as hereditary spherocytosis type 4 (HS4). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.<ref>PMID:8547122</ref> <ref>PMID:1378323</ref> <ref>PMID:7530501</ref> <ref>PMID:8943874</ref> <ref>PMID:8640229</ref> <ref>PMID:9207478</ref> <ref>PMID:9012689</ref> <ref>PMID:9233560</ref> <ref>PMID:9973643</ref> <ref>PMID:10580570</ref> <ref>PMID:10942416</ref> <ref>PMID:10745622</ref> <ref>PMID:11380459</ref> <ref>PMID:15813913</ref> <ref>PMID:16227998</ref>  Defects in SLC4A1 are the cause of renal tubular acidosis, distal, autosomal dominant (AD-dRTA) [MIM:[https://omim.org/entry/179800 179800]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.  Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA) [MIM:[https://omim.org/entry/611590 611590]]. A disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.  Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC) [MIM:[https://omim.org/entry/611590 611590]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.
== Function ==
[[https://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.
Architecture of the human erythrocyte ankyrin-1 complex.,Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865<ref>PMID:35835865</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v0y" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cali T]]
[[Category: Cali, T]]
[[Category: Clarke OB]]
[[Category: Clarke, O B]]
[[Category: Johnston JD]]
[[Category: Johnston, J D]]
[[Category: Kim K]]
[[Category: Kim, K]]
[[Category: Noble AJ]]
[[Category: Noble, A J]]
[[Category: Vallese F]]
[[Category: Vallese, F]]
[[Category: Yen LY]]
[[Category: Yen, L Y]]
[[Category: Ankyrin complex]]
[[Category: Erythrocyte]]
[[Category: Membrane protein]]
[[Category: Structural protein]]

Revision as of 21:19, 27 July 2022

Local refinement of Band 3-III cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complexLocal refinement of Band 3-III cytoplasmic domains, class 1 of erythrocyte ankyrin-1 complex

Structural highlights

7v0y is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[B3AT_HUMAN] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:109270]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.[1] [2] Defects in SLC4A1 are the cause of spherocytosis type 4 (SPH4) [MIM:612653]; also known as hereditary spherocytosis type 4 (HS4). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.[3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] Defects in SLC4A1 are the cause of renal tubular acidosis, distal, autosomal dominant (AD-dRTA) [MIM:179800]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA) [MIM:611590]. A disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC) [MIM:611590]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.

Function

[B3AT_HUMAN] Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin.

Publication Abstract from PubMed

The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.

Architecture of the human erythrocyte ankyrin-1 complex.,Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865[18]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT, Rubin HL, Zhai S, Sahr KE, Liu SC. Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11022-6. PMID:1722314
  2. ↑ Schofield AE, Tanner MJ, Pinder JC, Clough B, Bayley PM, Nash GB, Dluzewski AR, Reardon DM, Cox TM, Wilson RJ, et al.. Basis of unique red cell membrane properties in hereditary ovalocytosis. J Mol Biol. 1992 Feb 20;223(4):949-58. PMID:1538405
  3. ↑ Maillet P, Vallier A, Reinhart WH, Wyss EJ, Ott P, Texier P, Baklouti F, Tanner MJ, Delaunay J, Alloisio N. Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11. Br J Haematol. 1995 Dec;91(4):804-10. PMID:8547122
  4. ↑ Jarolim P, Palek J, Rubin HL, Prchal JT, Korsgren C, Cohen CM. Band 3 Tuscaloosa: Pro327----Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2. Blood. 1992 Jul 15;80(2):523-9. PMID:1378323
  5. ↑ Jarolim P, Rubin HL, Brabec V, Chrobak L, Zolotarev AS, Alper SL, Brugnara C, Wichterle H, Palek J. Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis. Blood. 1995 Feb 1;85(3):634-40. PMID:7530501
  6. ↑ Jarolim P, Murray JL, Rubin HL, Taylor WM, Prchal JT, Ballas SK, Snyder LM, Chrobak L, Melrose WD, Brabec V, Palek J. Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency. Blood. 1996 Dec 1;88(11):4366-74. PMID:8943874
  7. ↑ Eber SW, Gonzalez JM, Lux ML, Scarpa AL, Tse WT, Dornwell M, Herbers J, Kugler W, Ozcan R, Pekrun A, Gallagher PG, Schroter W, Forget BG, Lux SE. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet. 1996 Jun;13(2):214-8. PMID:8640229 doi:10.1038/ng0696-214
  8. ↑ Alloisio N, Texier P, Vallier A, Ribeiro ML, Morle L, Bozon M, Bursaux E, Maillet P, Goncalves P, Tanner MJ, Tamagnini G, Delaunay J. Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis. Blood. 1997 Jul 1;90(1):414-20. PMID:9207478
  9. ↑ Miraglia del Giudice E, Vallier A, Maillet P, Perrotta S, Cutillo S, Iolascon A, Tanner MJ, Delaunay J, Alloisio N. Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus. Br J Haematol. 1997 Jan;96(1):70-6. PMID:9012689
  10. ↑ Dhermy D, Galand C, Bournier O, Boulanger L, Cynober T, Schismanoff PO, Bursaux E, Tchernia G, Boivin P, Garbarz M. Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects. Br J Haematol. 1997 Jul;98(1):32-40. PMID:9233560
  11. ↑ Iwase S, Ideguchi H, Takao M, Horiguchi-Yamada J, Iwasaki M, Takahara S, Sekikawa T, Mochizuki S, Yamada H. Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis. Acta Haematol. 1998;100(4):200-3. PMID:9973643 doi:40904
  12. ↑ Lima PR, Sales TS, Costa FF, Saad ST. Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis. Eur J Haematol. 1999 Nov;63(5):360-1. PMID:10580570
  13. ↑ Ribeiro ML, Alloisio N, Almeida H, Gomes C, Texier P, Lemos C, Mimoso G, Morle L, Bey-Cabet F, Rudigoz RC, Delaunay J, Tamagnini G. Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3. Blood. 2000 Aug 15;96(4):1602-4. PMID:10942416
  14. ↑ Yawata Y, Kanzaki A, Yawata A, Doerfler W, Ozcan R, Eber SW. Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population. Int J Hematol. 2000 Feb;71(2):118-35. PMID:10745622
  15. ↑ Bracher NA, Lyons CA, Wessels G, Mansvelt E, Coetzer TL. Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III. Br J Haematol. 2001 Jun;113(3):689-93. PMID:11380459
  16. ↑ Lima PR, Baratti MO, Chiattone ML, Costa FF, Saad ST. Band 3Tambau: a de novo mutation in the AE1 gene associated with hereditary spherocytosis. Implications for anion exchange and insertion into the red blood cell membrane. Eur J Haematol. 2005 May;74(5):396-401. PMID:15813913 doi:10.1111/j.1600-0609.2004.00405.x
  17. ↑ Bruce LJ, Robinson HC, Guizouarn H, Borgese F, Harrison P, King MJ, Goede JS, Coles SE, Gore DM, Lutz HU, Ficarella R, Layton DM, Iolascon A, Ellory JC, Stewart GW. Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1. Nat Genet. 2005 Nov;37(11):1258-63. Epub 2005 Oct 9. PMID:16227998 doi:10.1038/ng1656
  18. ↑ Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB. Architecture of the human erythrocyte ankyrin-1 complex. Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865 doi:http://dx.doi.org/10.1038/s41594-022-00792-w

7v0y, resolution 3.00Å

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