1l5b: Difference between revisions

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[[Image:1l5b.~~gif~~|left|200px]]

[[Image:1l5b.png|left|200px]]

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~~'''~~DOMAIN-SWAPPED CYANOVIRIN-N DIMER~~'''~~

===DOMAIN-SWAPPED CYANOVIRIN-N DIMER===

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12015150}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12015150 is the PubMed ID number.

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==About this Structure==

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[[Category: Gp120]]

[[Category: Hiv-inactivating]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:33:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:44:07 2008''

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-[[Image:1l5b.gif|left|200px]]
+{{Seed}}
+[[Image:1l5b.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1l5b|  PDB=1l5b  |  SCENE=  }}
-'''DOMAIN-SWAPPED CYANOVIRIN-N DIMER'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12015150}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12015150 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12015150}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Gp120]]
 [[Category: Hiv-inactivating]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:33:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:44:07 2008''