Literature DB >> 1567428

Direct involvement of the C-terminal extremity of pancreatic lipase (403-449) in colipase binding.

C Chaillan1, B Kerfelec, E Foglizzo, C Chapus.   

Abstract

After a selective cleavage of a lipase/colipase cross-linked complex, the colipase has been shown to be bound to a 5 kDa lipase fragment identified as the C-terminal extremity of the chain extending from residue 403 to the C-terminus (Cys 449). The colipase binding site on lipase is therefore localized in a restricted contact area. Moreover, from sequence comparison of lipase from various species, an acidic residue, Glu 440, is likely to be involved in ion pairing with colipase.

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Year:  1992        PMID: 1567428     DOI: 10.1016/0006-291x(92)91179-t

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase.

Authors:  M P Egloff; L Sarda; R Verger; C Cambillau; H van Tilbeurgh
Journal:  Protein Sci       Date:  1995-01       Impact factor: 6.725

  1 in total

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