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1lom

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(New page: 200px<br /> <applet load="1lom" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lom, resolution 1.72&Aring;" /> '''CYANOVIRIN-N DOUBLE...)
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[[Image:1lom.gif|left|200px]]<br />
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[[Image:1lom.gif|left|200px]]<br /><applet load="1lom" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1lom" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1lom, resolution 1.72&Aring;" />
caption="1lom, resolution 1.72&Aring;" />
'''CYANOVIRIN-N DOUBLE MUTANT P51S S52P'''<br />
'''CYANOVIRIN-N DOUBLE MUTANT P51S S52P'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1LOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum] with SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LOM OCA].
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1LOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOM OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Botos, I.]]
[[Category: Botos, I.]]
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[[Category: Boyd, M.R.]]
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[[Category: Boyd, M R.]]
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[[Category: Cartner, L.K.]]
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[[Category: Cartner, L K.]]
[[Category: Mori, T.]]
[[Category: Mori, T.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
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[[Category: hiv-inactivating]]
[[Category: hiv-inactivating]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:17:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:53 2008''

Revision as of 11:46, 21 February 2008

Image:1lom.gif

1lom, resolution 1.72Å

Drag the structure with the mouse to rotate

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 with and as ligands. 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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