A differential geometric treatment of protein structure comparison.
The technique of model-building a protein of known sequence but unknown tertiary structure from the structures of homologous proteins is probably so far the most reliable means of mapping from primary to tertiary structure. A key step towards the realization of the aim is to develop ways of aligning three-dimensional structures of homologous proteins, thereby deriving the rules useful for protein modelling. We have developed a generalized differential-geometric representation of protein local conformation for use in a protein comparison program which aligns protein sequences on the basis of their sequence and conformational knowledge. Because the differential-geometric distance measure between local conformations is independent of the coordinate frame and remains chirality information, the comparison program is easily implemented, relatively rational and reasonably fast. The utility of this program for aligning closely and distantly related homologous proteins is demonstrated by multiple alignment of globins, serine proteinases and aspartic proteinase domains. Particularly, the method has reached the rational alignment between the mammalian and microbial serine proteinases as compared with many published alignment programs.
Ding
D F
DF
Laboratory of Computational Molecular Biology, Shanghai Institute of Biochemistry, Academia Sinica, China.
Qian
J
J
Feng
Z K
ZK
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry; D005914:Globins / Q000737:chemistry; D006801:Humans; D008433:Mathematics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry
D011506:Proteins; D005914:Globins; D012697:Serine Endopeptidases; D016282:Aspartic Acid Endopeptidases