7b01 | pdb_00007b01

ADAMTS13-CUB12

spinqualitylabelsall models 7b01, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: GLC, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Crystal structure of ADAMTS13 CUB domains reveals their role in global latency.,Kim HJ, Xu Y, Petri A, Vanhoorelbeke K, Crawley JTB, Emsley J Sci Adv. 2021 Apr 16;7(16). pii: 7/16/eabg4403. doi: 10.1126/sciadv.abg4403., Print 2021 Apr. PMID:33863735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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