View source for 4aog


==Solution structure of the Class II hydrophobin NC2==
<StructureSection load='4aog' size='340' side='right'caption='[[4aog]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aog]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa_OR74A Neurospora crassa OR74A]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AOG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=4aog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aog OCA], [https://pdbe.org/4aog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aog RCSB], [https://www.ebi.ac.uk/pdbsum/4aog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aog ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7S3P5_NEUCR Q7S3P5_NEUCR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydrophobins are fungal proteins that self-assemble spontaneously to form amphipathic monolayers at hydrophobic:hydrophilic interfaces. Hydrophobin assemblies facilitate fungal transitions between wet and dry environments and interactions with plant and animal hosts. NC2 is a previously uncharacterised hydrophobin from Neurospora crassa. It is a highly surface active protein and is able to form protein layers on a water:air interface that stabilise air bubbles. On a hydrophobic substrate, NC2 forms layers consisting of an ordered network of protein molecules which dramatically decrease the water contact angle. The solution structure and dynamics of NC2 have been determined using nuclear magnetic resonance spectroscopy. The structure of this protein displays the same core fold as observed in other hydrophobin structures determined to date, including the class II hydrophobins HFBI and HFBII from Trichoderma reesei, but certain features illuminate the structural differences between class I and class II hydrophobins and also highlight the variations between structures of class II hydrophobin family members. The unique properties of hydrophobins have attracted much attention for biotechnology applications. The insights obtained through determining the structure, biophysical properties and assembly characteristics of NC2 will facilitate the development of hydrophobin-based applications. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.

Solution structure and interface-driven self-assembly of NC2, a new member of the class II hydrophobin proteins.,Ren Q, Kwan AH, Sunde M Proteins. 2013 Nov 12. doi: 10.1002/prot.24473. PMID:24218020<ref>PMID:24218020</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aog" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Neurospora crassa OR74A]]
[[Category: Kwan AH]]
[[Category: Ren Q]]
[[Category: Sunde M]]