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Media type:
E-Article
Title:
Model for Haptoglobin Heavy Chain Based upon Structural Homology
Contributor:
Greer, Jonathan
Published:
National Academy of Sciences of the United States of America, 1980
Published in:
Proceedings of the National Academy of Sciences of the United States of America, 77 (1980) 6, Seite 3393-3397
Language:
English
ISSN:
0027-8424
Origination:
Footnote:
Description:
A model has been constructed for haptoglobin heavy chain by using the known sequence homology to the mammalian serine proteases. The three-dimensional structures for three serine proteases, chymotrypsin, trypsin, and elastase, were compared and the structural features that are conserved in all three were extracted. The haptoglobin heavy chain sequence was aligned to the sequences of the three serine proteases by maximizing sequence homology in the regions of conserved structure. The resulting alignment shows that haptoglobin heavy chain must be very closely homologous to these proteases in structure as well as in sequence. Coordinates were derived for the heavy chain by using the homologous structures. The problems associated with these coordinates are outlined and methods for solving them are indicated. The features of the haptoglobin heavy chain structure are described. Implications of the structure for the very strong interaction between this subunit and hemoglobin are discussed.