3tnu: Difference between revisions
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==Heterocomplex of coil 2B domains of human intermediate filament proteins, keratin 5 (KRT5) and keratin 14 (KRT14)== | ==Heterocomplex of coil 2B domains of human intermediate filament proteins, keratin 5 (KRT5) and keratin 14 (KRT14)== | ||
<StructureSection load='3tnu' size='340' side='right' caption='[[3tnu]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3tnu' size='340' side='right'caption='[[3tnu]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tnu]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tnu]] 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=3TNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TNU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.005Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tnu OCA], [https://pdbe.org/3tnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tnu RCSB], [https://www.ebi.ac.uk/pdbsum/3tnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tnu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== 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. | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3tnu" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Coulombe PA]] | ||
[[Category: | [[Category: Kim MS]] | ||
[[Category: | [[Category: Leahy DJ]] | ||
[[Category: | [[Category: Lee CH]] | ||
Latest revision as of 13:29, 6 November 2024
Heterocomplex of coil 2B domains of human intermediate filament proteins, keratin 5 (KRT5) and keratin 14 (KRT14)Heterocomplex of coil 2B domains of human intermediate filament proteins, keratin 5 (KRT5) and keratin 14 (KRT14)
Structural highlights
DiseaseK1C14_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. FunctionK1C14_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 PubMedThere is as yet no high-resolution data regarding the structure and organization of keratin intermediate filaments, which are obligate heteropolymers providing vital mechanical support in epithelia. We report the crystal structure of interacting 2B regions from the central coiled-coil domains of keratins 5 and 14 (K5 and K14), expressed in progenitor keratinocytes of epidermis. The interface of the K5-K14 coiled-coil heterodimer has asymmetric salt bridges, hydrogen bonds and hydrophobic contacts, and its surface exhibits a notable charge polarization. A trans-dimer homotypic disulfide bond involving Cys367 in K14's stutter region occurs in the crystal and in skin keratinocytes, where it is concentrated in a keratin filament cage enveloping the nucleus. We show that K14-Cys367 impacts nuclear shape in cultured keratinocytes and that mouse epidermal keratinocytes lacking K14 show aberrations in nuclear structure, highlighting a new function for keratin filaments. Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.,Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA Nat Struct Mol Biol. 2012 Jun 17;19(7):707-15. doi: 10.1038/nsmb.2330. PMID:22705788[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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