2MOP
Structure of Bitistatin A
Summary for 2MOP
| Entry DOI | 10.2210/pdb2mop/pdb |
| NMR Information | BMRB: 19947 |
| Descriptor | Disintegrin bitistatin (1 entity in total) |
| Functional Keywords | bitis arietans, snake venom, disintegrin, toxin |
| Biological source | Bitis arietans (African puff adder) |
| Cellular location | Secreted: P17497 |
| Total number of polymer chains | 1 |
| Total formula weight | 9014.02 |
| Authors | Carbajo, R.J.,Calvete, J.,Sanz, L.,Perez, A. (deposition date: 2014-04-29, release date: 2014-11-12, Last modification date: 2024-10-16) |
| Primary citation | Carbajo, R.J.,Sanz, L.,Perez, A.,Calvete, J.J. NMR structure of bitistatin - a missing piece in the evolutionary pathway of snake venom disintegrins. Febs J., 282:341-360, 2015 Cited by PubMed Abstract: Extant disintegrins, as found in the venoms of Viperidae and Crotalidae snakes (vipers and rattlesnakes, represent a family of polypeptides that block the function of β1 and β3 integrin receptors, both potently and with a high degree of selectivity. This toxin family owes its origin to the neofunctionalization of the extracellular region of an ADAM (a disintegrin and metalloprotease) molecule recruited into the snake venom gland proteome in the Jurassic. The evolutionary structural diversification of the disintegrin scaffold, from the ancestral long disintegrins to the more recently evolved medium-sized, dimeric and short disintegrins, involved the stepwise loss of pairs of class-specific disulfide linkages and the processing of the N-terminal region. NMR and crystal structures of medium-sized, dimeric and short disintegrins have been solved. However, the structure of a long disintegrin remained unknown. The present study reports the NMR solution structures of two disulfide bond conformers of the long disintegrin bitistatin from the African puff adder Bitis arietans. The findings provide insight into how a structural domain of the extracellular region of an ADAM molecule, recruited into and selectively expressed in the snake venom gland proteome as a PIII metalloprotease in the Jurassic, has subsequently been tranformed into a family of integrin receptor antagonists. PubMed: 25363287DOI: 10.1111/febs.13138 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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