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| | ==Structure of P51G Cyanovirin-N swapped trimer in the P212121 space group== | | ==Structure of P51G Cyanovirin-N swapped trimer in the P212121 space group== |
| - | <StructureSection load='4j4e' size='340' side='right' caption='[[4j4e]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4j4e' size='340' side='right'caption='[[4j4e]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j4e]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_variabilis_var._ellipsospora Anabaena variabilis var. ellipsospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J4E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j4e]] is a 6 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=4J4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J4E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j4c|4j4c]], [[4j4d|4j4d]], [[4j4f|4j4f]], [[4j4g|4j4g]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=4j4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4e OCA], [http://pdbe.org/4j4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j4e RCSB], [http://www.ebi.ac.uk/pdbsum/4j4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4e ProSAT]</span></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=4j4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4e OCA], [https://pdbe.org/4j4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j4e RCSB], [https://www.ebi.ac.uk/pdbsum/4j4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL]] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</ref> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena variabilis var. ellipsospora]] | + | [[Category: Large Structures]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Nostoc ellipsosporum]] |
| - | [[Category: Koharudin, L M.I]] | + | [[Category: Gronenborn AM]] |
| - | [[Category: Liu, L]] | + | [[Category: Koharudin LMI]] |
| - | [[Category: Antiviral protein]] | + | [[Category: Liu L]] |
| - | [[Category: Carbohydrate binding protein]]
| + | |
| - | [[Category: Cvnh fold]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
CVN_NOSEL Mannose-binding lectin.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boyd MR, Gustafson KR, McMahon JB, Shoemaker RH, O'Keefe BR, Mori T, Gulakowski RJ, Wu L, Rivera MI, Laurencot CM, Currens MJ, Cardellina JH 2nd, Buckheit RW Jr, Nara PL, Pannell LK, Sowder RC 2nd, Henderson LE. Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development. Antimicrob Agents Chemother. 1997 Jul;41(7):1521-30. PMID:9210678
- ↑ Botos I, Wlodawer A. Cyanovirin-N: a sugar-binding antiviral protein with a new twist. Cell Mol Life Sci. 2003 Feb;60(2):277-87. PMID:12678493
- ↑ Koharudin LM, Liu L, Gronenborn AM. Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates. Proc Natl Acad Sci U S A. 2013 Apr 22. PMID:23610431 doi:10.1073/pnas.1300327110
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