5wt7

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'''Unreleased structure'''
 
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The entry 5wt7 is ON HOLD until Paper Publication
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==FAS1-IV domain of Human Periostin==
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<StructureSection load='5wt7' size='340' side='right' caption='[[5wt7]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wt7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WT7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WT7 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wt7 OCA], [http://pdbe.org/5wt7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wt7 RCSB], [http://www.ebi.ac.uk/pdbsum/5wt7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wt7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Periostin, an extracellular matrix protein, is secreted by fibroblasts and is overexpressed in various types of cancers. The four internal repeat fasciclin 1 (FAS1) domains of human periostin play crucial roles in promoting tumor metastasis and progression via interaction with cell surface integrins. Among four FAS1 domains of human periostin, the fourth FAS1 domain (FAS1-IV) was prepared for NMR study, since only FAS1-IV was highly soluble, and showed a well-dispersed 2D (1)H-(15)N HSQC spectrum. Here, we report nearly complete backbone and side chain resonance assignments and a secondary structural analysis of the FAS1-IV domain as first steps toward the structure determination of FAS1-IV of human periostin.
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Authors: Yun, H., Lee, C.W.
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(1)H, (13)C, and (15)N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins.,Yun H, Kim EH, Lee CW Biomol NMR Assign. 2017 Oct 31. pii: 10.1007/s12104-017-9786-z. doi:, 10.1007/s12104-017-9786-z. PMID:29086898<ref>PMID:29086898</ref>
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Description: FAS1-IV domain of Human Periostin
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5wt7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Lee, C W]]
[[Category: Yun, H]]
[[Category: Yun, H]]
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[[Category: Lee, C.W]]
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[[Category: Cancer]]
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[[Category: Cell adhesion]]
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[[Category: Chronic allergic inflammation disease]]
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[[Category: Integrin]]
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[[Category: Periostin]]

Revision as of 07:00, 13 December 2017

FAS1-IV domain of Human Periostin

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