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| | <StructureSection load='6jfv' size='340' side='right'caption='[[6jfv]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6jfv' size='340' side='right'caption='[[6jfv]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jfv]] is a 4 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=6JFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JFV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jfv]] is a 4 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=6JFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JFV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KRT14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), KRT5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.6Å</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=6jfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfv OCA], [https://pdbe.org/6jfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jfv RCSB], [https://www.ebi.ac.uk/pdbsum/6jfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfv 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=6jfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfv OCA], [https://pdbe.org/6jfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jfv RCSB], [https://www.ebi.ac.uk/pdbsum/6jfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/K1C14_HUMAN K1C14_HUMAN]] Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Dermatopathia pigmentosa reticularis;Naegeli-Franceschetti-Jadassohn syndrome;Epidermolysis bullosa simplex with mottled pigmentation;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type;KRT14-related epidermolysis bullosa simplex. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[https://www.uniprot.org/uniprot/K2C5_HUMAN K2C5_HUMAN]] Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Epidermolysis bullosa simplex with circinate migratory erythema;Epidermolysis bullosa simplex with mottled pigmentation;Dowling-Degos disease;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
| + | [https://www.uniprot.org/uniprot/K1C14_HUMAN K1C14_HUMAN] Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Dermatopathia pigmentosa reticularis;Naegeli-Franceschetti-Jadassohn syndrome;Epidermolysis bullosa simplex with mottled pigmentation;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type;KRT14-related epidermolysis bullosa simplex. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/K1C14_HUMAN K1C14_HUMAN]] The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.<ref>PMID:11724817</ref>
| + | [https://www.uniprot.org/uniprot/K1C14_HUMAN K1C14_HUMAN] The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.<ref>PMID:11724817</ref> |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coulombe, P A]] | + | [[Category: Coulombe PA]] |
| - | [[Category: Kim, M S]] | + | [[Category: Kim MS]] |
| - | [[Category: Leahy, D J]] | + | [[Category: Leahy DJ]] |
| - | [[Category: Lee, C H]] | + | [[Category: Lee CH]] |
| - | [[Category: Cytosolic protein]]
| + | |
| - | [[Category: Epithelium]]
| + | |
| - | [[Category: Intermediate filament]]
| + | |
| - | [[Category: Keratinocyte]]
| + | |
| - | [[Category: Protein self-assembly]]
| + | |
| - | [[Category: Skin]]
| + | |
| Structural highlights
Disease
K1C14_HUMAN Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Dermatopathia pigmentosa reticularis;Naegeli-Franceschetti-Jadassohn syndrome;Epidermolysis bullosa simplex with mottled pigmentation;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type;KRT14-related epidermolysis bullosa simplex. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
Function
K1C14_HUMAN The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.[1]
Publication Abstract from PubMed
Intermediate filaments (IFs) provide vital mechanical support in a broad array of cell types. Interference with this role causes cell fragility and accounts for a large number of human diseases. Gaining an understanding of the structure of IFs is paramount to understanding their function and designing therapeutic agents for relevant diseases. Here, we report the 2.6-A resolution crystal structure of a complex of interacting 2B domains of keratin 5 (K5) and K14. K5 and K14 form a long-range, left-handed coiled coil, with participating alpha helices aligned in parallel and in register. Follow-up mutagenesis revealed that specific contacts between interacting 2B domains play a crucial role during 10-nm IF assembly, likely at the step of octamer-octamer association. The resulting structural model represents an atomic-resolution visualization of 2B-2B interactions important to filament assembly and provides insight into the defects introduced by mutations in IF genes associated with human skin diseases.
Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.,Lee CH, Kim MS, Li S, Leahy DJ, Coulombe PA Structure. 2020 Mar 3;28(3):355-362.e4. doi: 10.1016/j.str.2020.01.002. Epub 2020, Jan 28. PMID:31995743[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bousquet O, Ma L, Yamada S, Gu C, Idei T, Takahashi K, Wirtz D, Coulombe PA. The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro. J Cell Biol. 2001 Nov 26;155(5):747-54. Epub 2001 Nov 26. PMID:11724817 doi:http://dx.doi.org/10.1083/jcb.200104063
- ↑ Lee CH, Kim MS, Li S, Leahy DJ, Coulombe PA. Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly. Structure. 2020 Mar 3;28(3):355-362.e4. doi: 10.1016/j.str.2020.01.002. Epub 2020, Jan 28. PMID:31995743 doi:http://dx.doi.org/10.1016/j.str.2020.01.002
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