1l5b

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(New page: 200px<br /> <applet load="1l5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5b, resolution 2.00&Aring;" /> '''DOMAIN-SWAPPED CYAN...)
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<applet load="1l5b" size="450" color="white" frame="true" align="right" spinBox="true"
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'''DOMAIN-SWAPPED CYANOVIRIN-N DIMER'''<br />
'''DOMAIN-SWAPPED CYANOVIRIN-N DIMER'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1L5B 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 NA and NHE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L5B OCA].
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1L5B 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=NA:'>NA</scene> and <scene name='pdbligand=NHE:'>NHE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5B OCA].
==Reference==
==Reference==
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[[Category: Nostoc ellipsosporum]]
[[Category: Nostoc ellipsosporum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barrientos, L.G.]]
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[[Category: Barrientos, L G.]]
[[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: Gronenborn, A.M.]]
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[[Category: Gronenborn, A M.]]
[[Category: Han, Z.]]
[[Category: Han, Z.]]
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[[Category: Keefe, B.R.O.]]
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[[Category: Keefe, B R.O.]]
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[[Category: Louis, J.M.]]
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[[Category: Louis, J M.]]
[[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 14:16:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:28 2008''

Revision as of 11:41, 21 February 2008


1l5b, resolution 2.00Å

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DOMAIN-SWAPPED CYANOVIRIN-N DIMER

Overview

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.

About this Structure

1L5B is a Single protein structure of sequence from Nostoc ellipsosporum with and as ligands. Full crystallographic information is available from OCA.

Reference

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

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