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CATH - Protein
Structure Classification
Version 2.0 : Released Nov 2000
Dr. Frances M.G.
Pearl, Prof. Janet Thornton, Dr. Christine A. Orengo
Dr. Adrian
J. Shepherd, Dr. Andrew Harrison, Dr. David Lee
James Bray,
Annabel E. Todd, Ian Sillitoe, Daniel Buchan, Gabby Reeves
Options
Introduction
CATH is a novel
hierarchical classification of protein domain structures, which clusters
proteins at four major levels, Class(C),
Architecture(A),
Topology(T) and Homologous
superfamily (H).
Class, derived from secondary
structure content, is assigned for more than 90% of protein structures
automatically. Architecture, which describes the gross orientation of secondary
structures, independent of connectivities, is currently assigned manually.
The topology level clusters structures according to their toplogical connections
and numbers of secondary structures. The homologous superfamilies cluster
proteins with highly similar structures and functions. The assignments
of structures to toplogy families and homologous superfamilies are made
by sequence and structure comparisons.
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Click here for a more detailed explanation
Reference
Orengo, C.A., Michie,
A.D., Jones, S., Jones, D.T., Swindells, M.B., and Thornton, J.M. (1997)
CATH-
A Hierarchic Classification of Protein Domain Structures. Structure.
Vol 5. No 8. p.1093-1108.
Pearl, F.M.G, Lee, D., Bray,
J.E, Sillitoe, I., Todd, A.E., Harrison, A.P., Thornton, J.M. and Orengo,
C.A. (2000) Assigning genomic sequences to CATH Nucleic Acids Research.
Vol 28. No 1. 277-282
Authors
These WWW pages and the data on
which they are based are currently maintained by:-
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Dr. Frances Pearl1
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Mr. James Bray1
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Ms. Annabel Todd1
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Mr. Ian Sillitoe1
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Dr. Andrew Harrison1
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Prof. Janet Thornton1,6
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Dr. Christine Orengo1
Previous contributions are acknowledged
from:-
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Dr. S. Jones1
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Dr. A.D. Michie2
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Dr. M.B. Swindells2
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Dr. G. Hutchinson3
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Dr. D.T. Jones4
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Dr. Andrew Martin2
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Dr. Loredana Lo Conte 8
Thanks for advice and suggestions
from:-
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Dr. W.R. Taylor5
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Dr. R. Laskowski6
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Prof. J.S. Richardson7
1 - University College London
2 - Inpharmatica Ltd.
3 - Reading University
4 - Warwick University
5 - National Institute for
Medical Research, Mill Hill
6 - Birkbeck College, London
7 - Duke University, USA
8 - MRC LMB, Cambridge
Funding
This project has been developed
over many years and has been supported by:-
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U.K. Biotechnology and Biological
Sciences Research Council (BBSRC)
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U.K. Medical Research Council (Dr.
C.A. Orengo)
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European Union contract BIOT-CT91-0271
PL 890271
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The Wellcome Trust and The Royal
Society (Dr. D.T. Jones)
Acknowledgements
We acknowledge the contribution
of all experimentalists who have deposited their structures in the PDB.
We also acknowledge the effort of the staff at the Protein Data Bank for
maintaining the data.
We thank all our colleagues
in the BSM unit for their helpful discussions. |
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