1lom: Difference between revisions
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[[Image:1lom.gif|left|200px]] | [[Image:1lom.gif|left|200px]] | ||
'''CYANOVIRIN-N DOUBLE MUTANT P51S S52P''' | {{Structure | ||
|PDB= 1lom |SIZE=350|CAPTION= <scene name='initialview01'>1lom</scene>, resolution 1.72Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CYANOVIRIN-N DOUBLE MUTANT P51S S52P''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LOM is a [ | 1LOM is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12054761 12054761] | ||
[[Category: Nostoc ellipsosporum]] | [[Category: Nostoc ellipsosporum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hiv-inactivating]] | [[Category: hiv-inactivating]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:17 2008'' | ||
Revision as of 10:33, 20 March 2008
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| 1lom, resolution 1.72Å | |||||||||||||
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| Ligands: | SO4 and CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CYANOVIRIN-N DOUBLE MUTANT P51S S52P
Overview
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.
About this Structure
1LOM is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
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
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