Ontology highlight
ABSTRACT:
SUBMITTER: Scott EE
PROVIDER: S-EPMC263748 | biostudies-literature | 2003 Nov
REPOSITORIES: biostudies-literature
Scott Emily E EE He You Ai YA Wester Michael R MR White Mark A MA Chin Christopher C CC Halpert James R JR Johnson Eric F EF Stout C David CD
Proceedings of the National Academy of Sciences of the United States of America 20031016 23
The xenobiotic metabolizing cytochromes P450 (P450s) are among the most versatile biological catalysts known, but knowledge of the structural basis for their broad substrate specificity has been limited. P450 2B4 has been frequently used as an experimental model for biochemical and biophysical studies of these membrane proteins. A 1.6-A crystal structure of P450 2B4 reveals a large open cleft that extends from the protein surface directly to the heme iron between the alpha-helical and beta-sheet ...[more]