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Title
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Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.
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Authors
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E.F.Meyer,
R.Radhakrishnan,
G.M.Cole,
L.G.Presta.
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Ref.
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J Mol Biol, 1986,
189,
533-539.
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PubMed id
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Abstract
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A single crystal of porcine pancreatic elastase was mounted in a thin-walled
capillary and allowed to react with acetyl-Ala-Pro-Ala-paranitroanalide.
Diffraction data to 1.65 A resolution were measured and the isomorphous
structure was solved from the difference Fourier map. The structure contains two
surprises. Two molecules of the product: acetyl-Ala-Pro-Ala molecule are bound
in the extended binding site. Both molecules are bound backwards with respect to
the established mode of peptide binding.
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