Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3920
DC FieldValueLanguage
dc.contributor.authorMangani, Stefanoen_us
dc.contributor.authorP., Carlonien_us
dc.contributor.authorP., Oriolien_us
dc.date.accessioned2021-03-30T14:36:23Z-
dc.date.available2021-03-30T14:36:23Z-
dc.date.issued1992-
dc.identifier.issn0022-2836en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/3920-
dc.description47996en_US
dc.description.abstractThe X-ray crystal structure of the carboxypeptidase A-L-benzylsuccinate complex has been refined at 2.0 A resolution to a final R-factor of 0.166. One molecule of the inhibitor binds to the enzyme active site. The terminal carboxylate forms a salt link with the guanidinium group of Arg145 and hydrogen bonds with Tyr248 and Asn144. The second carboxylate group binds to the zinc ion in an asymmetric bidentate fashion replacing the water molecule of the native structure. The zinc ion moves 0.5 A from its position in the native structure to accommodate the inhibitor binding. The overall stereochemistry around the zinc can be considered a distorted tetrahedron, although six atoms of the co-ordinated groups lie within 3.0 A from the zinc ion. The key for the strong inhibitory properties of L-benzylsuccinate can be found in its ability both to co-ordinate the zinc and to form a short carboxyl-carboxylate-type hydrogen bond (2.5 A) with Glu270.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofJOURNAL OF MOLECULAR BIOLOGYen_US
dc.subjectx-ray; crystal structure; carboxypeptidase A; inhibitoren_US
dc.titleCrystal-structure of the Complex Between Carboxypeptidase-a and the Biproduct Analog Inhibitor L-benzylsuccinate At 2.0-a Resolutionen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/0022-2836(92)90671-6en_US
dc.identifier.pmid1738164en_US
dc.identifier.scopus2-s2.0-0026592667en_US
dc.identifier.isiWOS:A1992HB53400013en_US
dc.relation.volume223en_US
dc.relation.issue2en_US
dc.description.firstpage573en_US
dc.description.lastpage578en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-4824-7478-
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