Biomaterial Database

Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. 1993

H Atoda, and T Morita

Department of Biochemistry, Meiji College of Pharmacy, Tokyo.

Blood coagulation factor IX/factor X-binding protein (IX/X-bp) is a two-chain anticoagulant protein that was isolated from the venom of Trimeresurus flavoviridis. The amino acid sequence of IX/X-bp is homologous to the sequences of C-type lectin-like proteins, such as asialoglycoprotein receptor, tetranectin, and the low-affinity Fc epsilon receptor of immunoglobulin E. The amino acid composition and amino acid sequence of cystine-containing peptides, formed as a result of enzymatic digestion of CNBr-generated fragments of IX/X-bp, were analyzed to determine the location of the seven disulfide bridges in the protein. Three disulfide bridges in the A chain link Cys2 to Cys13, Cys30 to Cys127, and Cys102 to Cys119. Three disulfide bridges in the A chain link Cys2 to Cys13, Cys30 to Cys119, and Cys96 to Cys111. An interchain disulfide bond links Cys79 of the A chain and Cys75 of the B chain. The intrachain disulfide-bonding patterns of both the A and B chains of IX/X-bp are similar to those found in other C-type lectin-like proteins. We discuss in this report the sequence homology between IX/X-bp and other two-chain, C-type lectin-like proteins that have been isolated from snake venoms and we compare the S-S bonding patterns of proteins that are homologous to IX/X-bp.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003435	Crotalid Venoms	Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.	Bothrops Venom,Crotalidae Venoms,Pit Viper Venoms,Rattlesnake Venoms,Crotactin,Crotalid Venom,Crotalin,Crotaline Snake Venom,Crotalotoxin,Crotamin,Pit Viper Venom,Rattlesnake Venom,Snake Venom, Crotaline,Venom, Bothrops,Venom, Crotalid,Venom, Crotaline Snake,Venom, Pit Viper,Venom, Rattlesnake,Venoms, Crotalid,Venoms, Crotalidae,Venoms, Pit Viper,Venoms, Rattlesnake,Viper Venom, Pit
D004220	Disulfides	Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.	Disulfide
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino
D000925	Anticoagulants	Agents that prevent BLOOD CLOTTING.	Anticoagulant Agent,Anticoagulant Drug,Anticoagulant,Anticoagulant Agents,Anticoagulant Drugs,Anticoagulation Agents,Indirect Thrombin Inhibitors,Agent, Anticoagulant,Agents, Anticoagulant,Agents, Anticoagulation,Drug, Anticoagulant,Drugs, Anticoagulant,Inhibitors, Indirect Thrombin,Thrombin Inhibitors, Indirect
D030162	Reptilian Proteins	Proteins obtained from species of REPTILES.	Reptile Proteins