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The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain. The formation of a selenide-sulfide bond to form the cystine-like L-cysteinyl-L-selenocysteine, as in vertebrate selenopeptide P. The formation of a 2-keto-5-iminopiperazine protein chromophore cross-link from the alpha-amino nitrogen of residue n, a methionine, to the alpha-carboxyl carbon of residue n+1, a tyrosine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+2. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The posttranslation modification of two peptidyl-tyrosines to form a 3'-(O4'-L-tyrosinyl)-L-tyrosine protein cross-link. The formation of the non-fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamic acid, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like non-fluorescent red chromoprotein from the sea anemone Radianthus macrodactylus. The formation of the fluorescent protein FP611 chromophore cross-link from the alpha-carboxyl carbon of residue n, a methionine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like fluorescent chromoprotein from the sea anemone Entacmaea quadricolor. The posttranslational cross-linking of a tyrosine residue to a tryptophan residue and a methionine residue to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium. The posttranslational modification of peptidyl-lysine and peptidyl-serine to form a (2Xi,9S)-L-lysinoalanine cross-link. The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,4Xi,6R)-3-methyl-lanthionine sulfoxide (3-methyl-L-lanthionine sulfoxide), as found in the antibiotic actagardine. The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,6R)-3-methyl-lanthionine (3-methyl-L-lanthionine). The posttranslational synthesis of (S,Z)-S-(2-aminovinyl)cysteine forming an intra-polypeptide cross-link between serine and cysteine. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl glycine, or peptidyl cysteine-peptidyl glycine cross-link by the condensation of the serine hydroxyl or cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The formation of a protein active site cross-link from the alpha-carboxyl carbon of residue n, an alanine, serine or cysteine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with an oxidation of residue n+1 to form an active aldehyde. The posttranslation modification of peptidyl-histidine and peptidyl-tyrosine to form a protein cross-link. The formation of S-(peptidyl-glycyl)-peptidyl-cysteine cross-links by the formation of a thiolester between cysteine and the carboxy-terminal glycine of ubiquitin and other proteins. The posttranslational cross-linking of a cysteine residue to an L-phenylalanine residue to form 2-(S-L-cysteinyl)-L-phenylalanine. The posttranslational cross-linking of a tryptophan residue to tryptophyl quinone to form 4'-(L-tryptophan)-L-tryptophyl quinone, a cofactor found at the active site of methylamine dehydrogenase. The formation of the fluorescent protein FP583 chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The posttranslational thioether cross-linking of a cysteine residue to a tyrosine residue to form 3'-(S-L-cysteinyl)-L-tyrosine, found in galactose oxidase. The posttranslational cross-linking of a cysteine residue to an L-phenylalanine residue to form 2-(S-L-cysteinyl)-D-phenylalanine. The posttranslation modification of peptidyl-histidine and peptidyl-cysteine to form a 2'-(S-L-cysteinyl)-L-histidine protein cross-link. The posttranslation modification of peptidyl-glutamine and peptidyl-cysteine to form a S-(L-isoglutamyl)-L-cysteine protein cross-link. The post-translational cross-linking of a cysteine residue to an L-threonine residue to form 2-(S-L-cysteinyl)-D-allo-threonine. The posttranslational cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid. The oxidation of two peptidyl-cysteine residues to form a peptidyl-L-cystine (dicysteine) in which segments of peptide chain are linked by a disulfide bond; the cross-link may be between different or the same peptide chain. The posttranslational cross-linking of a cysteine residue to tryptophyl quinone to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone, a cofactor found at the active site of amine dehydrogenase. The posttranslational cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid. The posttranslation modification of two peptidyl-tyrosines to form a 3'-(3'-L-tyrosinyl)-L-tyrosine protein cross-link. The cross-linking of the epsilon-amino group of a peptidyl-lysine with peptidyl-topaquinone, a modified tyrosine residue. The posttranslational synthesis of (2R,6R)-lanthionine, sn-(2S,6R)-lanthionine or (2S,3S,6R)-3-methyl-lanthionine, forming an intra-polypeptide cross-link between peptidyl-cysteine, and peptidyl-serine or peptidyl-threonine; dehydration of the serine or threonine residue to the alpha,beta-unsaturated amino acid is the first step; a bond then forms between the ethylene (ethene) group thus formed and the sulfur atom of a cysteine, with the inversion of the configuration of the alpha carbon of the serine or threonine occurring during the process. The formation of a covalent cross-link between or within peptide chains, where either the amino group or the carboxyl group, or both, are not attached to the alpha carbon. The formation of a covalent cross-link between or within protein chains. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues. The formation of a cross-link between peptidyl-cysteine and peptidyl-threonine via the formation of S-(2-aminovinyl)-3-methyl-D-cysteine. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). The formation of 4-amino-3-isothiazolinone cross-links by the formation of a sulfenylamide bond between cysteine or cysteine sulfenic acid, and the alpha-amido of the following residue. The covalent alteration of one or more amino acids occurring in a protein after the protein has been completely translated and released from the ribosome.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptide cross-linking
Acc: GO:0018149
Aspect: Biological Process
Desc: The formation of a covalent cross-link between or within protein chains.
Proteins in PDR annotated with:
   This term: 35 [Search]
   Term or descendants: 46 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018149 - peptide cross-linking (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle