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• W173669577 abstract "Research Article1 October 1986free access X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. W. Bode W. Bode Search for more papers by this author A.Z. Wei A.Z. Wei Search for more papers by this author R. Huber R. Huber Search for more papers by this author E. Meyer E. Meyer Search for more papers by this author J. Travis J. Travis Search for more papers by this author S. Neumann S. Neumann Search for more papers by this author W. Bode W. Bode Search for more papers by this author A.Z. Wei A.Z. Wei Search for more papers by this author R. Huber R. Huber Search for more papers by this author E. Meyer E. Meyer Search for more papers by this author J. Travis J. Travis Search for more papers by this author S. Neumann S. Neumann Search for more papers by this author Author Information W. Bode, A.Z. Wei, R. Huber, E. Meyer, J. Travis and S. Neumann The EMBO Journal (1986)5:2453-2458https://doi.org/10.1002/j.1460-2075.1986.tb04521.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Orthorhombic crystals diffracting beyond 1.7 A resolution, have been grown from the stoichiometric complex formed between human leukocyte elastase (HLE) and the third domain of turkey ovomucoid inhibitor (OMTKY3). The crystal and molecular structure has been determined with the multiple isomorphous replacement technique. The complex has been modeled using the known structure of OMTKY3 and partial sequence information for HLE, and has been refined. The current crystallographic R-value is 0.21 for reflections from 25 to 1.8 A resolution. HLE shows the characteristic polypeptide fold of trypsin-like serine proteinases and consists of 218 amino acid residues. However, several loop segments, mainly arranged around the substrate binding site, have unique conformations. The largest deviations from the other vertebrate proteinases of known spatial structure are around Cys168. The specificity pocket is constricted by Val190, Val216 and Asp226 to preferentially accommodate medium sized hydrophobic amino acids at P1. Seven residues of the OMTKY3-binding segment are in specific contact with HLE. This interaction and geometry around the reactive site are similar as observed in other complexes. It is the first serine proteinase glycoprotein analysed, having two sugar chains attached to Asn159 and to residue 109. Previous ArticleNext Article Volume 5Issue 101 October 1986In this issue RelatedDetailsLoading ..." @default.
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• W173669577 title "X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor." @default.
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• W173669577 doi "https://doi.org/10.1002/j.1460-2075.1986.tb04521.x" @default.
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