The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
An open conformation of mammalian cytochrome P450 2B4 at 1.6-Å resolution
Open accessAbstract
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-Å crystal structure of P450 2B4 reveals a large open cleft that extends from the protein surface directly to the heme iron between the α-helical and β-sheet domains without perturbing the overall P450 fold. This cleft is primarily formed by helices B′ to C and F to G. The conformation of these regions is dramatically different from that of the other structurally defined mammalian P450, 2C5/3LVdH, in which the F to G and B′ to C regions encapsulate one side of the active site to produce a closed form of the enzyme. The open conformation of 2B4 is trapped by reversible formation of a homodimer in which the residues between helices F and G of one molecule partially fill the open cleft of a symmetry-related molecule, and an intermolecular coordinate bond occurs between H226 and the heme iron. This dimer is observed both in solution and in the crystal. Differences between the structures of 2C5 and 2B4 suggest that defined regions of xenobiotic metabolizing P450s may adopt a substantial range of energetically accessible conformations without perturbing the overall fold. This conformational flexibility is likely to facilitate substrate access, metabolic versatility, and product egress.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Phase annealing in SHELX-90: direct methods for larger structures
Sheldrick, G. M. (1990) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390000277 · Cited by 16,288
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. J. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,739
XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron Density
McRee, D. E. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4094 · Cited by 2,094
Summary of information on human CYP enzymes: human P450 metabolism data
Rendic, S. (2002) · Drug Metabolism Reviews · doi:10.1081/dmr-120001392 · Cited by 820
Mammalian Microsomal Cytochrome P450 Monooxygenase
Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696
Self-citationPodust, L. M., Poulos, T. L., & Waterman, M. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061562898 · Cited by 531
Structure of a cytochrome P450-redox partner electron-transfer complex
Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501
Li, H., & Poulos, T. L. (1997) · Nature Structural Biology · doi:10.1038/nsb0297-140 · Cited by 465
Cited by
Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., & Halpert, J. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403349200 · Cited by 279
Self-citationKim, J., & DellaPenna, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511207103 · Cited by 278
Structural basis for plant lutein biosynthesis from α-carotene
Niu, G., Guo, Q., Wang, J., Zhao, S., He, Y., & Liu, L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001806117 · Cited by 79
Self-citation
Metadata
- Authors
- Scott, E. E., He, Y. A., Wester, M. R., White, M. A., Chin, C. C., Halpert, J. R., Johnson, E. F., & Stout, C. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-10-16
- Volume
- 100
- Issue
- 23
- Pages
- 13196-13201
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2104180764
- Cited by
- 339
- References
- 25
- FWCI
- 23.93
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: An open conformation of mammalian cytochrome P450 2B4 at 1.6-Å resolution. https://app.cochat.ai/papers/10.1073/pnas.2133986100
- The paper
- Scott, E. E., He, Y. A., Wester, M. R., White, M. A., Chin, C. C., Halpert, J. R., Johnson, E. F., & Stout, C. D. (2003). An open conformation of mammalian cytochrome P450 2B4 at 1.6-Å resolution. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2133986100
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
