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1lom

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CYANOVIRIN-N DOUBLE MUTANT P51S S52P

Structural highlights

1lom is a 1 chain structure with sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.72Å
Ligands:	,
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

Cyanovirin-N (CV-N) is a potent 11 kDa HIV-inactivating protein that binds with high affinity to the HIV surface envelope protein gp120. A double mutant P51S/S52P of CV-N was engineered by swapping two critical hinge-region residues Pro51 and Ser52. This mutant has biochemical and biophysical characteristics equivalent to the wild-type CV-N and its structure resembles that of wild-type CV-N. However, the mutant shows a different orientation in the hinge region that connects two domains of the protein. The observation that this double mutant crystallizes under a wide variety of conditions challenges some of the current hypotheses on domain swapping and on the role of hinge-region proline residues in domain orientation. The current structure contributes to the understanding of domain swapping in cyanovirins, permitting rational design of domain-swapped CV-N mutants.

Domain-swapped structure of a mutant of cyanovirin-N.,Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761^[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
↑ Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A. Domain-swapped structure of a mutant of cyanovirin-N. Biochem Biophys Res Commun. 2002 May 31;294(1):184-90. PMID:12054761 doi:10.1016/S0006-291X(02)00455-2

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/1lom"

@@ Line 1: / Line 1: @@
 ==CYANOVIRIN-N DOUBLE MUTANT P51S S52P==
-<StructureSection load='1lom' size='340' side='right' caption='[[1lom]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
+<StructureSection load='1lom' size='340' side='right'caption='[[1lom]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lom]] is a 1 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=1LOM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LOM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lom]] is a 1 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=1LOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.72&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ezm|3ezm]], [[1l5b|1l5b]], [[1l5e|1l5e]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1lom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lom OCA], [http://pdbe.org/1lom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lom RCSB], [http://www.ebi.ac.uk/pdbsum/1lom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lom 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=1lom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lom OCA], [https://pdbe.org/1lom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lom RCSB], [https://www.ebi.ac.uk/pdbsum/1lom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lom 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1lom_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1lom_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Anabaena variabilis var. ellipsospora]]
+[[Category: Large Structures]]
-[[Category: Botos, I]]
+[[Category: Nostoc ellipsosporum]]
-[[Category: Boyd, M R]]
+[[Category: Botos I]]
-[[Category: Cartner, L K]]
+[[Category: Boyd MR]]
-[[Category: Mori, T]]
+[[Category: Cartner LK]]
-[[Category: Wlodawer, A]]
+[[Category: Mori T]]
-[[Category: Antiviral protein]]
+[[Category: Wlodawer A]]
-[[Category: Cyanovirin-n]]
-[[Category: Domain-swapping]]
-[[Category: Gp120]]
-[[Category: Hiv-inactivating]]

1lom

From Proteopedia

Current revision

CYANOVIRIN-N DOUBLE MUTANT P51S S52P

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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