Automated multiple structure alignment and detection of a common substructural motif

Proteins: Structure, Function and Genetics

Volumn 43, Issue 3, 2001, Pages 235-245

  Leibowitz, Nathaniel ^a   Fligelman, Zipora Y ^a   Nussinov, Ruth ^b   Wolfson, Haim J ^b  

^a TEL AVIV UNIVERSITY   (Israel)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Geometric hashing; Invariants; Multiple structural alignment; Multiple structural comparison; Structural core

Indexed keywords

PROTEIN;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; GEOMETRY; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

ALGORITHMS; AMINO ACID MOTIFS; AUTOMATION; GLOBINS; PROTEIN CONFORMATION; PROTEINS; TRIOSE-PHOSPHATE ISOMERASE;

EID: 0035874115     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1034     Document Type: Article

References (18)

1. Molecular surface representation by sparse critical points
2. Molecular recognition via face center representation of a molecular surface
3. Efficient detection of three-dimensional motifs in biological macromolecules by computer vision techniques
4. A structurally invariant core for the globins
5. Least squares fitting of two 3-D point set
6. H domains of immunoglobulin molecules
7. SSAP: Sequential structure alignment program for protein structure comparison
8. Using iterative dynamic programming to obtain accurate pairwise and multiple alignments if protein structures
9. Geometric Hashing: A general and efficient model-based recognition scheme
10. SCOP: A structural classification of proteins database for the investigation of sequences and structures
11. The protein databank: A computer-based archival file for macromolecular structures
12. A 3-D sequence-independent representation of the protein databank
13. HOMSTRAD: A database of protein structure alignments for homologous families
14. VMD - Visual molecular dynamics
15. Multiple structural alignment and core detection by geometric hashing
16. Conservation of polar residues as hot spots of protein interfaces
17. A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique