Vpr protein: Difference between revisions

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== Structural highlights<ref>PMID:12614620</ref> ==

Vpr structure is characterized by three well-defined α-helices: 17–33, 38–50 and 56–77 surrounded by flexible N and C-terminal domains. Vpr ~~have~~ been determined by NMR in the presence of 30% TFE several times, in [[1esx]], [[1vpc]] and [[1ceu]] structures. TFE is known to stabilize secondary structures and to prevent interactions between hydrophobic cores. However, the result was <scene name='75/750237/Vpr/1'>less globular structure</scene> than what it could be in reality. So, another NMR solution of Vpr was determined in the presence 10–30% of CD3CN, a less hydrophobic solvent, and in pure water. <scene name='75/750237/Vpr/2'>In this structure</scene> ([[1m8l]]), the structure folding around a hydrophobic core was improved, and can explain the binding properties of Vpr.

Vpr structure is characterized by three well-defined α-helices: 17–33, 38–50 and 56–77 surrounded by flexible N and C-terminal domains. Vpr has been determined by NMR in the presence of 30% TFE several times, in [[1esx]], [[1vpc]] and [[1ceu]] structures. TFE is known to stabilize secondary structures and to prevent interactions between hydrophobic cores. However, the result was <scene name='75/750237/Vpr/1'>less globular structure</scene> than what it could be in reality. So, another NMR solution of Vpr was determined in the presence 10–30% of CD3CN, a less hydrophobic solvent, and in pure water. <scene name='75/750237/Vpr/2'>In this structure</scene> ([[1m8l]]), the structure folding around a hydrophobic core was improved, and can explain the binding properties of Vpr.

== Conservation ==

Vpr protein: Difference between revisions

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@@ Line 17: / Line 17: @@
 == Structural highlights<ref>PMID:12614620</ref> ==
-Vpr structure is characterized by three well-defined α-helices: 17–33, 38–50 and 56–77 surrounded by flexible N and C-terminal domains. Vpr have been determined by NMR in the presence of 30% TFE several times, in [[1esx]], [[1vpc]] and [[1ceu]] structures. TFE is known to stabilize secondary structures and to prevent interactions between hydrophobic cores. However, the result was <scene name='75/750237/Vpr/1'>less globular structure</scene> than what it could be in reality. So, another NMR solution of Vpr was determined in the presence 10–30% of CD3CN, a less hydrophobic solvent, and in pure water. <scene name='75/750237/Vpr/2'>In this structure</scene> ([[1m8l]]), the structure folding around a hydrophobic core was improved, and can explain the binding properties of Vpr.
+Vpr structure is characterized by three well-defined α-helices: 17–33, 38–50 and 56–77 surrounded by flexible N and C-terminal domains. Vpr has been determined by NMR in the presence of 30% TFE several times, in [[1esx]], [[1vpc]] and [[1ceu]] structures. TFE is known to stabilize secondary structures and to prevent interactions between hydrophobic cores. However, the result was <scene name='75/750237/Vpr/1'>less globular structure</scene> than what it could be in reality. So, another NMR solution of Vpr was determined in the presence 10–30% of CD3CN, a less hydrophobic solvent, and in pure water. <scene name='75/750237/Vpr/2'>In this structure</scene> ([[1m8l]]), the structure folding around a hydrophobic core was improved, and can explain the binding properties of Vpr.
 == Conservation ==