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1ay6
From Proteopedia
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THROMBIN INHIBITOR FROM THEONALLA, CYCLOTHEANAMIDE-BASED MACROCYCLIC TRIPEPTIDE MOTIF
Overview
The macrocyclic peptide cyclotheonamide A (CtA), isolated from the marine, sponge Theonella sp., represents an unusual class of serine protease, inhibitor. A complex of this inhibitor with human alpha-thrombin, a, protease central to the bioregulation of thrombosis and hemostasis, was, studied by x-ray crystallography. This work (2.3-A resolution) confirms, the structure of CtA and reveals intimate details about its molecular, recognition within the enzyme active site. Interactions due to the, "Pro-Arg motif" (Arg occupancy of the S1 specificity pocket; formation of, a hydrogen-bonded two-strand antiparallel beta-sheet with Ser214-Gly216), and the alpha-keto amide group of CtA are primarily responsible for, binding to thrombin, with the alpha-keto amide serving as a, transition-state ... [(full description)]
About this Structure
1AY6 is a [Protein complex] structure of sequences from [Homo sapiens] with HHO as [ligand]. Active as [[1]], with EC number [3.4.21.5]. Full crystallographic information is available from [OCA].
Reference
Molecular basis for the inhibition of human alpha-thrombin by the macrocyclic peptide cyclotheonamide A., Maryanoff BE, Qiu X, Padmanabhan KP, Tulinsky A, Almond HR Jr, Andrade-Gordon P, Greco MN, Kauffman JA, Nicolaou KC, Liu A, et al., Proc Natl Acad Sci U S A. 1993 Sep 1;90(17):8048-52. PMID:8367461
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