About: Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver

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About: Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver
Creator	Arolas, Joan Avilés, Francesc Gomis-Rüth, F Guevara, Tibisay Lorenzo, Julia Tanco, Sebastián
Source	Elsevier; Medline; PMC
abstract	Abstract Drosophila melanogaster silver gene is the ortholog of the coding gene of mammalian carboxypeptidase D (CPD). The silver gene gives rise to eight different splicing variants of differing length that can contain up to three homologous repeats. Among the protein variants encoded, the short form 1B alias DmCPD1Bs (D . melanogaster CPD variant 1B short) is necessary and sufficient for viability of the fruit fly. It has one single repeat, it is active against standard peptide substrates, and it is localized to the secretory pathway. In this work, the enzyme was found as a monomer in solution and as a homodimer in the crystal structure, which features a protomer with an N-terminal 311-residue catalytic domain of α/β-hydrolase fold and a C-terminal 84-residue all-β transthyretin-like domain. Overall, DmCPD1Bs conforms to the structure of N/E-type funnelins/M14B metallopeptidases, but it has two unique structural elements potentially involved in regulation of its activity: (i) two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus providing control through localization, and (ii) a surface hot spot targetable by peptidases that would provide a regulatory mechanism through proteolytic inactivation. Given that the fruit fly possesses orthologs of only two out of the five proteolytically competent N/E-type funnelins found in higher vertebrates, DmCPD1Bs may represent a functional analog of at least one of the missing mammalian CPs.
has issue date	2010-08-20(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2010.06.035
bibo:pmid	20600119
has license	els-covid
sha1sum (hex)	41be0d9fde3eda13f0db87f085f8af260a468b5e
schema:url	https://doi.org/10.1016/j.jmb.2010.06.035
resource representing a document's title	Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver
has PubMed Central identifier	PMC7089606
has PubMed identifier	20600119
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:41be0d9fde3eda13f0db87f085f8af260a468b5e#body_text
is schema:about of	named entity 'Drosophila melanogaster' named entity 'enzyme' named entity 'coding' named entity 'hot spot' named entity 'unique' named entity 'Splicing' named entity 'SUFFICIENT' named entity 'MISSING' named entity 'FUNCTIONAL' named entity 'CPD' named entity 'MELANOGASTER' named entity 'GIVEN' named entity 'CYSTEINES' named entity 'CONTROL' named entity 'VARIANT' named entity 'CARBOXYPEPTIDASE D' named entity 'MECHANISM' named entity 'CONTAIN' named entity 'NECESSARY' named entity 'CATALYTIC DOMAIN' named entity 'UNIQUE' named entity 'RESIDUE' named entity 'POSSESSES' named entity 'ALIAS' named entity 'REPRESENT' named entity 'SURFACE' named entity 'STRUCTURE' named entity 'DROSOPHILA MELANOGASTER' named entity 'SPLICING VARIANT' named entity 'CODING' named entity 'STRUCTURAL' named entity 'VARIANTS' named entity 'VIABILITY' named entity 'BUT' named entity 'FEATURES' named entity 'ACTIVITY' named entity 'DIFFERENT' named entity 'FUNCTION ANALYSIS' named entity 'CARBOXYPEPTIDASE' named entity 'SILVER' named entity 'ENCODED' named entity 'RISE' named entity 'ELEMENTS' named entity 'SILVER' named entity 'MONOMER' named entity 'ORTHOLOG' named entity 'SOLUTION' named entity 'PROTEOLYTIC' named entity 'DOMAIN' named entity 'TYPE' named entity 'FORM' named entity 'FOLD' named entity 'REGULATORY' named entity 'GENE' named entity 'PEPTIDASES' named entity 'CONFORMS' named entity 'COMPETENT' named entity 'HYDROLASE' named entity 'LOCALIZATION' named entity 'LIKE' named entity 'HOMOLOGOUS' named entity 'OVERALL' named entity 'TARGET' named entity 'ITS' named entity 'SHORT' named entity 'VERTEBRATES' named entity '311' named entity 'SHORT' named entity 'TRANSTHYRETIN' named entity 'N-TERMINAL ' named entity 'ACTIVE' named entity 'PROVIDE' named entity 'PEPTIDE' named entity 'METALLOPEPTIDASES' named entity 'REPEAT' named entity 'ENCODED'

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