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| | <StructureSection load='6a9p' size='340' side='right'caption='[[6a9p]], [[Resolution|resolution]] 2.51Å' scene=''> | | <StructureSection load='6a9p' size='340' side='right'caption='[[6a9p]], [[Resolution|resolution]] 2.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6a9p]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6A9P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a9p]] is a 8 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=6A9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A9P FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6a9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9p OCA], [http://pdbe.org/6a9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9p RCSB], [http://www.ebi.ac.uk/pdbsum/6a9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9p ProSAT]</span></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]] 2.51Å</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=6a9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9p OCA], [https://pdbe.org/6a9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a9p RCSB], [https://www.ebi.ac.uk/pdbsum/6a9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/GFAP_HUMAN GFAP_HUMAN]] Alexander disease type I;Alexander disease type II. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/GFAP_HUMAN GFAP_HUMAN] Alexander disease type I;Alexander disease type II. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GFAP_HUMAN GFAP_HUMAN]] GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. | + | [https://www.uniprot.org/uniprot/GFAP_HUMAN GFAP_HUMAN] GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jin, M S]] | + | [[Category: Jin MS]] |
| - | [[Category: Kim, B]] | + | [[Category: Kim B]] |
| - | [[Category: Kim, S]] | + | [[Category: Kim S]] |
| - | [[Category: 1b domain]]
| + | |
| - | [[Category: Alexander disease]]
| + | |
| - | [[Category: Glial fibrillary acidic protein. gfap]]
| + | |
| - | [[Category: If]]
| + | |
| - | [[Category: Intermediate filament]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Disease
GFAP_HUMAN Alexander disease type I;Alexander disease type II. The disease is caused by mutations affecting the gene represented in this entry.
Function
GFAP_HUMAN GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells.
Publication Abstract from PubMed
Glial fibrillary acidic protein (GFAP) is a homopolymeric type III intermediate filament (IF) that plays essential roles in cell migration, mitosis, development, and signaling in astrocytes and a specific type of glial cells. Its overexpression and genetic mutations lead to abnormal IF networks and accumulation of Rosenthal fibers, which results in the fatal neurodegenerative disorder Alexander disease. Herein, we present the first crystal structure of human GFAP spanning the central coiled-coil 1B domain at 2.5A resolution. The domain forms a tetramer comprising two equivalent parallel coiled-coil dimers that pack together in an antiparallel manner. Its assembly is stabilized by extensive networks of intermolecular hydrogen bonds, salt bridges, and hydrophobic interactions. Furthermore, mapping of the GFAP mutations associated with Alexander disease reveals that most involve residues buried in the core of the interface, and are likely to disrupt the intermolecular interactions and/or introduce steric clashes, thereby decreasing GFAP solubility and promoting aggregation. Based on our structural analysis and previous biochemical studies, we propose that GFAP assembles in the A11 mode in which coiled-coil 1B dimers lie in close axial proximity in an antiparallel fashion to provide a stable tetrameric platform for the organization of the GFAP filament.
Crystal structure of the human glial fibrillary acidic protein 1B domain.,Kim B, Kim S, Jin MS Biochem Biophys Res Commun. 2018 Sep 18;503(4):2899-2905. doi:, 10.1016/j.bbrc.2018.08.066. Epub 2018 Aug 17. PMID:30126635[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim B, Kim S, Jin MS. Crystal structure of the human glial fibrillary acidic protein 1B domain. Biochem Biophys Res Commun. 2018 Sep 18;503(4):2899-2905. doi:, 10.1016/j.bbrc.2018.08.066. Epub 2018 Aug 17. PMID:30126635 doi:http://dx.doi.org/10.1016/j.bbrc.2018.08.066
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