2hn8

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{{STRUCTURE_2hn8| PDB=2hn8 | SCENE= }}
{{STRUCTURE_2hn8| PDB=2hn8 | SCENE= }}
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'''Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein'''
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===Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein===
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==Overview==
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Recently, a novel 87-amino acid influenza A virus protein with proapoptotic properties, PB1-F2, has been reported that originates from an alternative reading frame in the PB1 polymerase gene and is encoded in most known human influenza A virus isolates. Here we characterize the molecular structure of a biologically active synthetic version of the protein (sPB1-F2). Western blot analysis, chemical cross-linking, and NMR spectroscopy afforded direct evidence of the inherent tendency of sPB1-F2 to undergo oligomerization mediated by two distinct domains located in the N and C termini, respectively. CD and (1)H NMR spectroscopic analyses indicate that the stability of structured regions in the molecule clearly depends upon the hydrophobicity of the solvent. In aqueous solutions, the behavior of sPB1-F2 is typical of a largely random coil peptide that, however, adopts alpha-helical structure upon the addition of membrane mimetics. (1)H NMR analysis of three overlapping peptides afforded, for the first time, direct experimental evidence of the presence of a C-terminal region with strong alpha-helical propensity comprising amino acid residues Ile(55)-Lys(85) connected via an essentially random coil structure to a much weaker helix-like region, located in the N terminus between residues Trp(9) and Lys(20). The C-terminal helix is not a true amphipathic helix and is more compact than previously predicted. It corresponds to a positively charged region previously shown to include the mitochondrial targeting sequence of PB1-F2. The consequences of the strong oligomerization and helical propensities of the molecule are discussed and used to formulate a hypothetical model of its interaction with the mitochondrial membrane.
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(as it appears on PubMed at http://www.pubmed.gov), where 17052982 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17052982}}
==About this Structure==
==About this Structure==
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2HN8 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HN8 OCA].
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2HN8 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HN8 OCA].
==Reference==
==Reference==
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[[Category: Wray, V.]]
[[Category: Wray, V.]]
[[Category: Pro-apoptotic mitochondrial targeting protein]]
[[Category: Pro-apoptotic mitochondrial targeting protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:20:53 2008''

Revision as of 02:20, 29 July 2008

Image:2hn8.png

Template:STRUCTURE 2hn8

Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein

Template:ABSTRACT PUBMED 17052982

About this Structure

2HN8 is a Single protein structure. Full experimental information is available from OCA.

Reference

Structural characterization and oligomerization of PB1-F2, a proapoptotic influenza A virus protein., Bruns K, Studtrucker N, Sharma A, Fossen T, Mitzner D, Eissmann A, Tessmer U, Roder R, Henklein P, Wray V, Schubert U, J Biol Chem. 2007 Jan 5;282(1):353-63. Epub 2006 Oct 19. PMID:17052982

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