1ss6
Solution structure of SEP domain from human p47Solution structure of SEP domain from human p47
Structural highlights
FunctionNSF1C_HUMAN Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) (By similarity). Inhibits the activity of CTSL (in vitro). Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of the human p47 SEP domain in a construct comprising residues G1-S2-p47(171-270) was determined by NMR spectroscopy. A structure-derived hypothesis about the domains' function was formulated and pursued in binding experiments with cysteine proteases. The SEP domain was found to be a reversible competitive inhibitor of cathepsin L with a Ki of 1.5 microM. The binding of G1-S2-p47(171-270) to cathepsin L was mapped by biochemical assays and the binding interface was investigated by NMR chemical shift perturbation experiments. The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L.,Soukenik M, Diehl A, Leidert M, Sievert V, Bussow K, Leitner D, Labudde D, Ball LJ, Lechner A, Nagler DK, Oschkinat H FEBS Lett. 2004 Oct 22;576(3):358-62. PMID:15498563[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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