1l5e

<StructureSection load='1l5e' size='340' side='right'caption='[[1l5e]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1l5e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_variabilis_var._ellipsospora Anabaena variabilis var. ellipsospora]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L5E FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ezm|2ezm]], [[3ezm|3ezm]], [[1l5b|1l5b]]</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=1l5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5e OCA], [http://pdbe.org/1l5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l5e RCSB], [http://www.ebi.ac.uk/pdbsum/1l5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5e ProSAT]</span></td></tr>

[[http://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 ==

The structure of the potent HIV-inactivating protein cyanovirin-N was previously found by NMR to be a monomer in solution and a domain-swapped dimer by X-ray crystallography. Here we demonstrate that, in solution, CV-N can exist both in monomeric and in domain-swapped dimeric form. The dimer is a metastable, kinetically trapped structure at neutral pH and room temperature. Based on orientational NMR constraints, we show that the domain-swapped solution dimer is similar to structures in two different crystal forms, exhibiting solely a small reorientation around the hinge region. Mutation of the single proline residue in the hinge to glycine significantly stabilizes the protein in both its monomeric and dimeric forms. By contrast, mutation of the neighboring serine to proline results in an exclusively dimeric protein, caused by a drastic destabilization of the monomer.

The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.,Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM Structure. 2002 May;10(5):673-86. PMID:12015150<ref>PMID:12015150</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1l5e" style="background-color:#fffaf0;"></div>

[[Category: Anabaena variabilis var. ellipsospora]]

[[Category: Barrientos, L G]]

[[Category: Botos, I]]

[[Category: Boyd, M R]]

[[Category: Gronenborn, A M]]

[[Category: Han, Z]]

[[Category: Keefe, B R.O]]

[[Category: Louis, J M]]

[[Category: Mori, T]]

[[Category: Wlodawer, A]]

[[Category: 3d domain-swapping]]

[[Category: Protein folding]]