View source for 5yjh


==Structural insights into periostin functions==
<StructureSection load='5yjh' size='340' side='right'caption='[[5yjh]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yjh]] 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=5YJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YJH 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]] 2.957&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5yjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yjh OCA], [https://pdbe.org/5yjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yjh RCSB], [https://www.ebi.ac.uk/pdbsum/5yjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yjh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POSTN_HUMAN POSTN_HUMAN] Induces cell attachment and spreading and plays a role in cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity).[UniProtKB:Q62009]<ref>PMID:12235007</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human periostin plays a multifaceted role in remodeling the extracellular matrix milieu by interacting with other proteins and itself in both a heterophilic and homophilic manner. However, the structural mechanism for its extensive interactions has remained elusive. Here, we report the crystal structures of human periostin (EMI-Fas1(I-)(IV) ) and its Cys60Ala mutant. In combination with multi-angle light-scattering analysis and biochemical assays, the crystal structures reveal that periostin mainly exists as a dimer in solution and its homophilic interaction is mainly mediated by the EMI domain. Furthermore, Cys60 undergoes cysteinylation as confirmed by mass spectroscopy, and this site hardly affects the homophilic interaction. Also, the structures yield insights into how periostin forms heterophilic interactions with other proteins under physiological or pathological conditions.

Structural characterizations of human periostin dimerization and cysteinylation.,Liu J, Zhang J, Xu F, Lin Z, Li Z, Liu H FEBS Lett. 2018 Jun;592(11):1789-1803. doi: 10.1002/1873-3468.13091. Epub 2018, May 21. PMID:29754429<ref>PMID:29754429</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yjh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Liu H]]
[[Category: Liu J]]
[[Category: Xu F]]