View source for 2hm3


==Nematocyst outer wall antigen, cysteine rich domain NW1==
<StructureSection load='2hm3' size='340' side='right'caption='[[2hm3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hm3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HM3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 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=2hm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hm3 OCA], [https://pdbe.org/2hm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hm3 RCSB], [https://www.ebi.ac.uk/pdbsum/2hm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hm3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8IT70_HYDVU Q8IT70_HYDVU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nematocyst wall of cnidarians is a unique biomaterial that withstands extreme osmotic pressures, allowing an ultrafast discharge of the nematocyst capsules. Assembly of the highly robust nematocyst wall is achieved by covalent linkage of cysteine-rich domains (CRDs) from two main protein components, minicollagens and nematocyst outer wall antigen (NOWA). The bipolar minicollagens have different disulfide patterns and topologies in their N and C-terminal CRDs. The functional significance of this polarity has been elusive. Here, we show by NMR structural analysis that all representative cysteine-rich domains of NOWA are structurally related to N-terminal minicollagen domains. Natural sequence insertions in NOWA CRDs have very little effect on the tightly knit domain structures, nor do they preclude the efficient folding to a single native conformation. The different folds in NOWA CRDs and the atypical C-terminal minicollagen domain on the other hand can be directly related to different conformational preferences in the reduced states. Ultrastructural analysis in conjunction with aggregation studies argues for an association between the similar NOWA and N-terminal minicollagen domains in early stages of the nematocyst wall assembly, which is followed by the controlled association between the unusual structures of C-terminal minicollagen domains.

Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall.,Meier S, Jensen PR, Adamczyk P, Bachinger HP, Holstein TW, Engel J, Ozbek S, Grzesiek S J Mol Biol. 2007 May 4;368(3):718-28. Epub 2007 Feb 24. PMID:17362991<ref>PMID:17362991</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hm3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Hydra vulgaris]]
[[Category: Large Structures]]
[[Category: Grzesiek S]]
[[Category: Jensen PR]]
[[Category: Meier S]]
[[Category: Oezbek S]]