1ss6 | pdb_00001ss6
From Proteopedia
Solution structure of SEP domain from human p47
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Structural highlights
Evolutionary Conservation![]() Check, 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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This page was last modified 16:54, 29 September 2014.