View source for 4j4d


==Structure of P51G Cyanovirin-N swapped dimer in the P21212 space group==
<StructureSection load='4j4d' size='340' side='right'caption='[[4j4d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j4d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J4D 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&#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=4j4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4d OCA], [https://pdbe.org/4j4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j4d RCSB], [https://www.ebi.ac.uk/pdbsum/4j4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although it has long been established that the amino acid sequence encodes the fold of a protein, how individual proteins arrive at their final conformation is still difficult to predict, especially for oligomeric structures. Here, we present a comprehensive characterization of oligomeric species of cyanovirin-N that all are formed by a polypeptide chain with the identical amino acid sequence. Structures of the oligomers were determined by X-ray crystallography, and each one exhibits 3D domain swapping. One unique 3D domain-swapped structure is observed for the trimer, while for both dimer and tetramer, two different 3D domain-swapped structures were obtained. In addition to the previously identified hinge-loop region of the 3D domain-swapped dimer, which resides between strands beta5 and beta6 in the middle of the polypeptide sequence, another hinge-loop region is observed between strands beta7 and beta8 in the structures. Plasticity in these two regions allows for variability in dihedral angles and concomitant differences in chain conformation that results in the differently 3D domain-swapped multimers. Based on all of the different structures, we propose possible folding pathways for this protein. Altogether, our results illuminate the amazing ability of cyanovirin-N to proceed down different folding paths and provide general insights into oligomer formation via 3D domain swapping.

Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates.,Koharudin LM, Liu L, Gronenborn AM Proc Natl Acad Sci U S A. 2013 Apr 22. PMID:23610431<ref>PMID:23610431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4j4d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nostoc ellipsosporum]]
[[Category: Gronenborn AM]]
[[Category: Koharudin LMI]]
[[Category: Liu L]]