3ud2: Difference between revisions

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[[Image:3ud2.png|left|200px]]
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{{STRUCTURE_3ud2|  PDB=3ud2  |  SCENE=  }}  
{{STRUCTURE_3ud2|  PDB=3ud2  |  SCENE=  }}  
===Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin===
===Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin===
{{ABSTRACT_PUBMED_22310050}}


==Disease==
[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:[http://omim.org/entry/182900 182900]]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.<ref>PMID:8640229</ref><ref>PMID:11102985</ref>


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==Function==
The line below this paragraph, {{ABSTRACT_PUBMED_22310050}}, adds the Publication Abstract to the page
[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.<ref>PMID:12456646</ref>  Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.<ref>PMID:12456646</ref>  
(as it appears on PubMed at http://www.pubmed.gov), where 22310050 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22310050}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:022310050</ref><references group="xtra"/>
<ref group="xtra">PMID:022310050</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ipsaro, J J.]]
[[Category: Ipsaro, J J.]]

Revision as of 00:58, 25 March 2013

Template:STRUCTURE 3ud2

Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrinCrystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin

Template:ABSTRACT PUBMED 22310050

DiseaseDisease

[ANK1_HUMAN] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:182900]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.[1][2]

FunctionFunction

[ANK1_HUMAN] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.[3] Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.[4]

About this StructureAbout this Structure

3ud2 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. ↑ Yasunaga M, Ipsaro JJ, Mondragon A. Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin. J Mol Biol. 2012 Jan 30. PMID:22310050 doi:http://dx.doi.org/10.1016/j.jmb.2012.01.041
  1. ↑ 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
  2. ↑ Leite RC, Basseres DS, Ferreira JS, Alberto FL, Costa FF, Saad ST. Low frequency of ankyrin mutations in hereditary spherocytosis: identification of three novel mutations. Hum Mutat. 2000 Dec;16(6):529. PMID:11102985 doi:<529::AID-HUMU13>3.0.CO;2-N 10.1002/1098-1004(200012)16:6<529::AID-HUMU13>3.0.CO;2-N
  3. ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
  4. ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646

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