7B01
ADAMTS13-CUB12
Summary for 7B01
| Entry DOI | 10.2210/pdb7b01/pdb |
| Descriptor | Maltodextrin-binding protein,Maltodextrin-binding protein,Maltodextrin-binding protein,ADAMTS13 CUB12,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | adamts13, cub, metalloprotease, hydrolase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 1 |
| Total formula weight | 67309.03 |
| Authors | Kim, H.J.,Emsley, J. (deposition date: 2020-11-18, release date: 2021-04-28, Last modification date: 2024-01-31) |
| Primary citation | Kim, H.J.,Xu, Y.,Petri, A.,Vanhoorelbeke, K.,Crawley, J.T.B.,Emsley, J. Crystal structure of ADAMTS13 CUB domains reveals their role in global latency. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: ADAMTS13 is a plasma metalloprotease that is essential for the regulation of von Willebrand factor (VWF) function, mediator of platelet recruitment to sites of blood vessel damage. ADAMTS13 function is dynamically regulated by structural changes induced by VWF binding that convert it from a latent to active conformation. ADAMTS13 global latency is manifest by the interaction of its C-terminal CUB1-2 domains with its central Spacer domain. We resolved the crystal structure of the ADAMTS13 CUB1-2 domains revealing a previously unreported configuration for the tandem CUB domains. Docking simulations between the CUB1-2 domains with the Spacer domain in combination with enzyme kinetic functional characterization of ADAMTS13 CUB domain mutants enabled the mapping of the CUB1-2 domain site that binds the Spacer domain. Together, these data reveal the molecular basis of the ADAMTS13 Spacer-CUB interaction and the control of ADAMTS13 global latency. PubMed: 33863735DOI: 10.1126/sciadv.abg4403 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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