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1l5e

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Revision as of 06:39, 18 August 2021

The domain-swapped dimer of CV-N in solution

Structural highlights

1l5e is a 2 chain structure with sequence from Anabaena variabilis var. ellipsospora. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ezm, 3ezm, 1l5b
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CVN_NOSEL] Mannose-binding lectin.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l5e"

@@ Line 3: / Line 3: @@
 <StructureSection load='1l5e' size='340' side='right'caption='[[1l5e]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1l5e]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ezm|2ezm]], [[3ezm|3ezm]], [[1l5b|1l5b]]</div></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5e OCA], [https://pdbe.org/1l5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l5e RCSB], [https://www.ebi.ac.uk/pdbsum/1l5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5e ProSAT]</span></td></tr>
 </table>
 == 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1l5e

From Proteopedia

Revision as of 06:39, 18 August 2021

The domain-swapped dimer of CV-N in solution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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