1xm9
From Proteopedia
(Difference between revisions)
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<StructureSection load='1xm9' size='340' side='right'caption='[[1xm9]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1xm9' size='340' side='right'caption='[[1xm9]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xm9]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1xm9]] is a 1 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=1XM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XM9 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]] 2.8Å</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=1xm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xm9 OCA], [https://pdbe.org/1xm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1xm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xm9 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PKP1_HUMAN PKP1_HUMAN] Defects in PKP1 are the cause of ectodermal dysplasia-skin fragility syndrome (EDSFS) [MIM:[https://omim.org/entry/604536 604536]; also known as McGrath syndrome. Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. EDSFS is characterized by features of both cutaneous fragility and congenital ectodermal dysplasia affecting abnormalities in other epithelia or tissues. Desmosomes in the skin are small and poorly formed with widening of keratinocyte intercellular spaces and perturbed desmosome/keratin intermediate filament interactions. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PKP1_HUMAN PKP1_HUMAN] Seems to play a role in junctional plaques. Contributes to epidermal morphogenesis. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xm9 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xm9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The p120ctn subfamily of armadillo domain proteins has roles in modulating intercellular adhesion by cadherin-containing junctions. We have determined the crystal structure of the arm repeat domain from plakophilin-1 (PKP1), a member of the p120ctn subfamily that is found in desmosomes. The structure reveals that the domain has nine instead of the expected ten arm repeats. A sequence predicted to be an arm repeat is instead a large insert which serves as a wedge that produces a significant bend in the overall domain structure. Structure-based sequence alignments indicate that the nine repeats and large insert are common to this subfamily of armadillo proteins. A prominent basic patch on the surface of the protein may serve as a binding site for partners of these proteins. | ||
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| - | Structure of the armadillo repeat domain of plakophilin 1.,Choi HJ, Weis WI J Mol Biol. 2005 Feb 11;346(1):367-76. Epub 2004 Dec 19. PMID:15663951<ref>PMID:15663951</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1xm9" style="background-color:#fffaf0;"></div> | ||
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| - | ==See Also== | ||
| - | *[[Armadillo repeats|Armadillo repeats]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Choi | + | [[Category: Choi HJ]] |
| - | [[Category: Weis | + | [[Category: Weis WI]] |
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Current revision
Structure of the armadillo repeat domain of plakophilin 1
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