Literature DB >> 3640831

Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.

E F Meyer, R Radhakrishnan, G M Cole, L G Presta.   

Abstract

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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Year:  1986        PMID: 3640831     DOI: 10.1016/0022-2836(86)90322-0

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  5 in total

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2.  Energy minimization and molecular dynamics studies of Asn-102 elastase.

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Authors:  John L Kulp; Ian S Cloudsdale; John L Kulp; Frank Guarnieri
Journal:  PLoS One       Date:  2017-08-24       Impact factor: 3.240

5.  S46 peptidases are the first exopeptidases to be members of clan PA.

Authors:  Yasumitsu Sakamoto; Yoshiyuki Suzuki; Ippei Iizuka; Chika Tateoka; Saori Roppongi; Mayu Fujimoto; Koji Inaka; Hiroaki Tanaka; Mika Masaki; Kazunori Ohta; Hirofumi Okada; Takamasa Nonaka; Yasushi Morikawa; Kazuo T Nakamura; Wataru Ogasawara; Nobutada Tanaka
Journal:  Sci Rep       Date:  2014-05-15       Impact factor: 4.379

  5 in total

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