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Title
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Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg.
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Authors
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C.A.McPhalen,
H.P.Schnebli,
M.N.James.
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Ref.
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Febs Lett, 1985,
188,
55-58.
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PubMed id
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Abstract
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The crystal structure of the molecular complex of eglin, a serine proteinase
inhibitor from leeches, with subtilisin Carlsberg has been determined at 2.0 A
resolution by the molecular replacement method. The complex has been refined by
restrained-parameter least-squares. The present crystallographic R factor
(Formula: see text) is 0.183. Eglin is a member of the potato inhibitor 1
family, a group of serine proteinase inhibitors lacking disulfide bonds. Eglin
shows strong structural homology to CI-2, a related inhibitor from barley seeds.
The structure of subtilisin Carlsberg in this complex is very similar to the
known structure from barley seeds. The structure of subtilisin Carlsberg in this
complex is very similar to the known structure of subtilisin novo, despite
changes of 84 out of 274 amino acids.
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