Structural highlights
Function
CAPSD_BPPF1 Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity).
Publication Abstract from PubMed
At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints.
Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and lambda-Maps.,Park SH, Son WS, Mukhopadhyay R, Valafar H, Opella SJ J Am Chem Soc. 2009 Sep 17. PMID:19761238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Park SH, Son WS, Mukhopadhyay R, Valafar H, Opella SJ. Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and lambda-Maps. J Am Chem Soc. 2009 Sep 17. PMID:19761238 doi:10.1021/ja905640d
