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| | <StructureSection load='1gg3' size='340' side='right'caption='[[1gg3]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1gg3' size='340' side='right'caption='[[1gg3]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gg3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GG3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gg3]] is a 3 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=1GG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GG3 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;'>[[1ef1|1ef1]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=1gg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gg3 OCA], [https://pdbe.org/1gg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1gg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gg3 ProSAT]</span></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=1gg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gg3 OCA], [https://pdbe.org/1gg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1gg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gg3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/41_HUMAN 41_HUMAN]] Defects in EPB41 are the cause of elliptocytosis type 1 (EL1) [MIM:[https://omim.org/entry/611804 611804]]. EL1 is a Rhesus-linked 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. Defects in EPB41 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[https://omim.org/entry/266140 266140]]. HPP is an autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.
| + | [https://www.uniprot.org/uniprot/EPB41_HUMAN EPB41_HUMAN] Hereditary elliptocytosis. The disease is caused by variants affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/41_HUMAN 41_HUMAN]] Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes.
| + | [https://www.uniprot.org/uniprot/EPB41_HUMAN EPB41_HUMAN] Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127).<ref>PMID:23870127</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Han, B G]] | + | [[Category: Han BG]] |
| - | [[Category: Blood]]
| + | |
| - | [[Category: Calmodulin]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: N-terminal domain]]
| + | |
| Structural highlights
Disease
EPB41_HUMAN Hereditary elliptocytosis. The disease is caused by variants affecting the gene represented in this entry.
Function
EPB41_HUMAN Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the core domain (N-terminal 30 kDa domain) of cytoskeletal protein 4.1R has been determined and shows a cloverleaf-like architecture. Each lobe of the cloverleaf contains a specific binding site for either band 3, glycophorin C/D or p55. At a central region of the molecule near where the three lobes are joined are two separate calmodulin (CaM) binding regions. One of these is composed primarily of an alpha-helix and is Ca 2+ insensitive; the other takes the form of an extended structure and its binding with CaM is dramatically enhanced by the presence of Ca 2+, resulting in the weakening of protein 4.1R binding to its target proteins. This novel architecture, in which the three lobes bind with three membrane associated proteins, and the location of calmodulin binding sites provide insight into how the protein 4.1R core domain interacts with membrane proteins and dynamically regulates cell shape in response to changes in intracellular Ca2+ levels.
Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization.,Han BG, Nunomura W, Takakuwa Y, Mohandas N, Jap BK Nat Struct Biol. 2000 Oct;7(10):871-5. PMID:11017195[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kiyomitsu T, Cheeseman IM. Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase. Cell. 2013 Jul 18;154(2):391-402. PMID:23870127 doi:10.1016/j.cell.2013.06.010
- ↑ Han BG, Nunomura W, Takakuwa Y, Mohandas N, Jap BK. Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization. Nat Struct Biol. 2000 Oct;7(10):871-5. PMID:11017195 doi:10.1038/82819
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