| 词条 | Barwin domain |
| 释义 |
| Symbol = Barwin | Name = Barwin | image = PDB 1bw4 EBI.jpg | width = | caption = three-dimensional structure in solution of barwin, a protein from barley seed | Pfam = PF00967 | Pfam_clan = CL0199 | InterPro = IPR001153 | SMART = | PROSITE = PDOC00619 | MEROPS = | SCOP = 1bw3 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, the barwin domain is a protein domain found in barwin, a basic protein isolated from aqueous extracts of barley seeds. Barwin is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges.[1][2] Comparative analysis shows the sequence of barwin to be highly similar to a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2) from potato, the product of the hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco. The high levels of similarity to these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants. References1. ^{{cite journal |vauthors=Svensson B, Svendsen I, Hojrup P, Roepstorff P, Ludvigsen S, Poulsen FM | title = Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes | journal = Biochemistry | volume = 31 | issue = 37 | pages = 8767–70 |date=September 1992 | pmid = 1390663 | doi = 10.1021/bi00152a012 | url = }} {{InterPro content|IPR001153}}2. ^{{cite journal |vauthors=Ludvigsen S, Poulsen FM | title = Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy | journal = Biochemistry | volume = 31 | issue = 37 | pages = 8771–82 |date=September 1992 | pmid = 1390664 | doi = 10.1021/bi00152a013 | url = }} 1 : Protein domains |
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