View source for 7wdl


==Fungal immunomodulatory protein FIP-nha==
<StructureSection load='7wdl' size='340' side='right'caption='[[7wdl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wdl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_solani Fusarium solani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WDL 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]] 1.903&#8491;</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=7wdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wdl OCA], [https://pdbe.org/7wdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wdl RCSB], [https://www.ebi.ac.uk/pdbsum/7wdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wdl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C7ZE17_FUSV7 C7ZE17_FUSV7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fungal immunomodulatory proteins (FIPs) have been investigated for their use as potential natural derived anti-tumor molecules. However, the stability of FIPs is critical for their preparation and storage. In this study, the correlation between thermal stability and protein structural features of rFIP-nha, with significant anti-tumor activity, has been evaluated. For comprehensive analysis, FIP-nha and its homologues FIP-gmi, FIP-fve, and LZ-8 were all recombinantly expressed in E. coli. In solution, rFIP-nha and rFIP-gmi formed tetramers; rFIP-fve and rLZ-8 appeared as dimers. Their melting temperatures were 85.1 degrees C, 77.8 degrees C, 66.5 degrees C, and 64.4 degrees C, respectively. Accordingly, their cytotoxicity was also temperature dependent. To investigate the underlying mechanism of their thermostability, we solved the crystal structure of FIP-nha. Detailed structure analysis, molecular dynamic simulation and mutagenesis studies indicated that a higher thermostability was correlated to higher oligomerization states, larger interface area, and more interactions. The structure property studies indicate that Y12, D61 and Y108 were critical for oligomerization and high thermostability of rFIP-nha, but the dimeric and tetrameric states of rFIP-nha exert similar cytotoxicity on A549 cells. Taken together, these findings reveal that thermostability of FIPs was dependent on their oligomerization state, and correlated with their cytotoxicity.

Linking the thermostability of FIP-nha (Nectria haematococca) to its structural properties.,Liu Y, Bastiaan-Net S, Zhang Y, Hoppenbrouwers T, Xie Y, Wang Y, Wei X, Du G, Zhang H, Imam KMDSU, Wichers H, Li Z Int J Biol Macromol. 2022 Jul 31;213:555-564. doi: , 10.1016/j.ijbiomac.2022.05.136. Epub 2022 May 26. PMID:35644318<ref>PMID:35644318</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wdl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fusarium solani]]
[[Category: Large Structures]]
[[Category: Bastiaan-Net S]]
[[Category: Du G]]
[[Category: Hoppenbrouwers T]]
[[Category: Imam KMSU]]
[[Category: Li Z]]
[[Category: Liu Y]]
[[Category: Wang Y]]
[[Category: Wei X]]
[[Category: Wichers HJ]]
[[Category: Xie Y]]
[[Category: Zhang H]]
[[Category: Zhang Y]]