The four cysteines ring motif in proteins.
Disulfide bonds play fundamental roles in proteins. This work is devoted to highly rare motifs containing disulfide bonds. A search for four cysteines, forming a 16-atom membered ring (4CR) embodying two disulfide bonds, was carried out against all entries in the Protein Data Bank. Searching the crystallographic subset, only few protein molecules, all dimeric, were found to embody this peculiar structural feature, which establishes a covalent link between two different polypeptide chains. In contrast, in a peptide studied in solution by NMR, the four cysteines moiety includes only residues from one chain. A comparative analysis provided evidence for similarity and difference. It emerged that 4CR motif is highly rare and may serve to gain a specialized function.
Zagari
Adriana
A
Dipartimento delle Scienze Biologiche, Università degli Studi di Napoli, Via Mezzocannone 16, Naples, Italy. adriana.zagari@unina.it
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D002417:Cattle; D002645:Chickens; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry*; D030562:Databases, Protein; D004220:Disulfides / Q000737:chemistry; D004722:Endoribonucleases / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008958:Models, Molecular; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D001426:Bacterial Proteins; D004220:Disulfides; D006360:Heat-Shock Proteins; C113725:HspA protein, bacteria; D011506:Proteins; D005340:Fibrinogen; D004722:Endoribonucleases; C032523:ribonuclease SPL; D003545:Cysteine