2c55
From Proteopedia
(New page: 200px<br /> <applet load="2c55" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c55" /> '''SOLUTION STRUCTURE OF THE HUMAN IMMUNODEFIC...) |
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'''SOLUTION STRUCTURE OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 P6 PROTEIN'''<br /> | '''SOLUTION STRUCTURE OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 P6 PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human immunodeficiency virus type 1 p6 protein represents a docking | + | The human immunodeficiency virus type 1 p6 protein represents a docking site for several cellular and viral binding factors and fulfills major roles in the formation of infectious viruses. To date, however, the structure of this 52-amino acid protein, by far the smallest lentiviral protein known, either in its mature form as free p6 or as the C-terminal part of the Pr55 Gag polyprotein has not been unraveled. We have explored the high resolution structure and folding of p6 by CD and NMR spectroscopy. Under membranous solution conditions, p6 can adopt a helix-flexible helix structure; a short helix-1 (amino acids 14-18) is connected to a pronounced helix-2 (amino acids 33-44) by a flexible hinge region. Thus, p6 can be subdivided into two distinct structural and functional domains; helix-2 perfectly defines the region that binds to the virus budding factor AIP-1/ALIX, indicating that this structure is required for interaction with the endosomal sorting complex required for transport. The PTAP motif at the N terminus, comprising the primary late assembly domain, which is crucial for interaction with another cellular budding factor, Tsg101, does not exhibit secondary structure. However, the adjacent helix-1 may play an indirect role in the specific complex formation between p6 and the binding groove in Tsg101. Moreover, binding studies by NMR demonstrate that helix-2, which also comprises the LXXLF motif required for incorporation of the human immunodeficiency virus type 1 accessory protein Vpr into budding virions, specifically interacts with the Vpr binding region, indicating that under the specific solution conditions used for structure analysis, p6 adopted a functional conformation. |
==About this Structure== | ==About this Structure== | ||
| - | 2C55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 2C55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C55 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:07 2008'' |
Revision as of 14:45, 21 February 2008
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SOLUTION STRUCTURE OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 P6 PROTEIN
Overview
The human immunodeficiency virus type 1 p6 protein represents a docking site for several cellular and viral binding factors and fulfills major roles in the formation of infectious viruses. To date, however, the structure of this 52-amino acid protein, by far the smallest lentiviral protein known, either in its mature form as free p6 or as the C-terminal part of the Pr55 Gag polyprotein has not been unraveled. We have explored the high resolution structure and folding of p6 by CD and NMR spectroscopy. Under membranous solution conditions, p6 can adopt a helix-flexible helix structure; a short helix-1 (amino acids 14-18) is connected to a pronounced helix-2 (amino acids 33-44) by a flexible hinge region. Thus, p6 can be subdivided into two distinct structural and functional domains; helix-2 perfectly defines the region that binds to the virus budding factor AIP-1/ALIX, indicating that this structure is required for interaction with the endosomal sorting complex required for transport. The PTAP motif at the N terminus, comprising the primary late assembly domain, which is crucial for interaction with another cellular budding factor, Tsg101, does not exhibit secondary structure. However, the adjacent helix-1 may play an indirect role in the specific complex formation between p6 and the binding groove in Tsg101. Moreover, binding studies by NMR demonstrate that helix-2, which also comprises the LXXLF motif required for incorporation of the human immunodeficiency virus type 1 accessory protein Vpr into budding virions, specifically interacts with the Vpr binding region, indicating that under the specific solution conditions used for structure analysis, p6 adopted a functional conformation.
About this Structure
2C55 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of the human immunodeficiency virus type 1 p6 protein., Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U, J Biol Chem. 2005 Dec 30;280(52):42515-27. Epub 2005 Oct 17. PMID:16234236
Page seeded by OCA on Thu Feb 21 16:45:07 2008
Categories: Single protein | Bruns, K. | Fossen, T. | Henklein, P. | Klinger, P. | Maczurek, A. | Rachmat, J. | Schubert, U. | Tessmer, U. | Wray, V. | Aids | Core protein | Hiv-1 | Lipoprotein | Membrane | Metal-binding | Myristate | P6 | P6-gag | Phosphorylation | Polyprotein | Rna-binding | Viral nucleoprotein | Viral protein | Zinc | Zinc-finger
