2asa

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HOMOLOGY MODELING OF CYTOCHROME P450SCCHOMOLOGY MODELING OF CYTOCHROME P450SCC

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

A new homology model of bovine cytochrome P450scc is obtained starting from the recently determined crystal structure of mammalian cytochrome P450 2B4. The new emerging structure appears compatible with recent diffraction patterns of bovine P450scc microcrystals as obtained at the Microfocus Beamline of the European Synchrotron Radiation in Grenoble and here reported for the first time. The same atomic structure is utilized thereby to predict the mutations needed for modifying redox potential. A comprehensive comparison is finally carried out with the previous model present in the RCSB Protein DataBank also in terms of the alternative mutations being predicted for the same functional modification. The implication of these studies for optimal sensor construction is discussed.

Homology modeling of cytochrome P450scc and the mutations for optimal amperometric sensor.,Sivozhelezov V, Nicolini C J Theor Biol. 2005 Jun 21;234(4):479-85. PMID:15808869^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sivozhelezov V, Nicolini C. Homology modeling of cytochrome P450scc and the mutations for optimal amperometric sensor. J Theor Biol. 2005 Jun 21;234(4):479-85. PMID:15808869 doi:10.1016/j.jtbi.2004.12.008

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OCA

[1] Sivozhelezov V, Nicolini C. Homology modeling of cytochrome P450scc and the mutations for optimal amperometric sensor. J Theor Biol. 2005 Jun 21;234(4):479-85. PMID:15808869 doi:10.1016/j.jtbi.2004.12.008

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