View source for 4pcw


==Crystal Structure of the N-terminal Domain of Human Profilaggrin at 2.2 A Resolution==
<StructureSection load='4pcw' size='340' side='right'caption='[[4pcw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pcw]] 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=4PCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PCW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4pcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pcw OCA], [https://pdbe.org/4pcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pcw RCSB], [https://www.ebi.ac.uk/pdbsum/4pcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pcw ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/FILA_HUMAN FILA_HUMAN] Autosomal dominant ichthyosis vulgaris. The disease is caused by mutations affecting the gene represented in this entry.  Disease susceptibility is associated with variations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/FILA_HUMAN FILA_HUMAN] Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis.
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== Publication Abstract from PubMed ==
The fused-type S100 protein profilaggrin and its proteolytic products including filaggrin are important in the formation of a normal epidermal barrier; however, the specific function of the S100 calcium-binding domain in profilaggrin biology is poorly understood. To explore its molecular function, we determined a 2.2 A-resolution crystal structure of the N-terminal fused-type S100 domain of human profilaggrin with bound calcium ions. The profilaggrin S100 domain formed a stable dimer, which contained two hydrophobic pockets that provide a molecular interface for protein interactions. Biochemical and molecular approaches demonstrated that three proteins, annexin II/p36, stratifin/14-3-3 sigma, and Hsp27, bind to the N-terminal domain of human profilaggrin; one protein (stratifin) co-localized with profilaggrin in the differentiating granular cell layer of human skin. Together, these findings suggest a model where the profilaggrin N-terminus uses calcium-dependent and calcium-independent protein-protein interactions to regulate its involvement in keratinocyte terminal differentiation and incorporation into the cornified cell envelope.Journal of Investigative Dermatology accepted article preview online, 11 March 2015. doi:10.1038/jid.2015.102.

Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin and hsp27.,Bunick CG, Presland RB, Lawrence OT, Pearton DJ, Milstone LM, Steitz TA J Invest Dermatol. 2015 Mar 11. doi: 10.1038/jid.2015.102. PMID:25760235<ref>PMID:25760235</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bunick CG]]
[[Category: Steitz TA]]