Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1996 Jan 1;24(1):201–205. doi: 10.1093/nar/24.1.201

The HSSP database of protein structure-sequence alignments.

R Schneider 1, C Sander 1
PMCID: PMC145595  PMID: 8594579

Abstract

HSSP is a derived database merging structural three dimensional (3-D) and sequence one dimensional(1-D) information. For each protein of known 3-D structure from the Protein Data Bank (PDB), the database has a multiple sequence alignment of all available homologues and a sequence profile characteristic of the family. The list of homologues is the result of a database search in Swissprot using a position-weighted dynamic programming method for sequence profile alignment (MaxHom). The database is updated frequently. The listed homologues are very likely to have the same 3-D structure as the PDB protein to which they have been aligned. As a result, the database is not only a database of aligned sequence families, but also a database of implied secondary and tertiary structures covering 27% of all Swissprot-stored sequences.

Full Text

The Full Text of this article is available as a PDF (177.4 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bairoch A., Boeckmann B. The SWISS-PROT protein sequence data bank. Nucleic Acids Res. 1992 May 11;20 (Suppl):2019–2022. doi: 10.1093/nar/20.suppl.2019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bernstein F. C., Koetzle T. F., Williams G. J., Meyer E. F., Jr, Brice M. D., Rodgers J. R., Kennard O., Shimanouchi T., Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol. 1977 May 25;112(3):535–542. doi: 10.1016/s0022-2836(77)80200-3. [DOI] [PubMed] [Google Scholar]
  3. Casari G., Andrade M. A., Bork P., Boyle J., Daruvar A., Ouzounis C., Schneider R., Tamames J., Valencia A., Sander C. Challenging times for bioinformatics. Nature. 1995 Aug 24;376(6542):647–648. doi: 10.1038/376647a0. [DOI] [PubMed] [Google Scholar]
  4. Hobohm U., Scharf M., Schneider R., Sander C. Selection of representative protein data sets. Protein Sci. 1992 Mar;1(3):409–417. doi: 10.1002/pro.5560010313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Holm L., Sander C. Database algorithm for generating protein backbone and side-chain co-ordinates from a C alpha trace application to model building and detection of co-ordinate errors. J Mol Biol. 1991 Mar 5;218(1):183–194. doi: 10.1016/0022-2836(91)90883-8. [DOI] [PubMed] [Google Scholar]
  6. Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol. 1993 Sep 5;233(1):123–138. doi: 10.1006/jmbi.1993.1489. [DOI] [PubMed] [Google Scholar]
  7. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 1983 Dec;22(12):2577–2637. doi: 10.1002/bip.360221211. [DOI] [PubMed] [Google Scholar]
  8. Rost B., Sander C., Schneider R. PHD--an automatic mail server for protein secondary structure prediction. Comput Appl Biosci. 1994 Feb;10(1):53–60. doi: 10.1093/bioinformatics/10.1.53. [DOI] [PubMed] [Google Scholar]
  9. Rost B., Schneider R., Sander C. Progress in protein structure prediction? Trends Biochem Sci. 1993 Apr;18(4):120–123. doi: 10.1016/0968-0004(93)90017-h. [DOI] [PubMed] [Google Scholar]
  10. Sander C., Schneider R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins. 1991;9(1):56–68. doi: 10.1002/prot.340090107. [DOI] [PubMed] [Google Scholar]
  11. Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph. 1990 Mar;8(1):52-6, 29. doi: 10.1016/0263-7855(90)80070-v. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES