1SS6

Solution structure of SEP domain from human p47

Summary for 1SS6

• Entry DOI: 10.2210/pdb1ss6/pdb
• NMR Information: BMRB: 6189
• Descriptor: NSFL1 cofactor p47 (1 entity in total)
• Functional Keywords: nmr; p47; sep, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (By similarity): Q9UNZ2
• Total number of polymer chains: 1
• Total formula weight: 11367.58

Authors

Soukenik, M.,Leidert, M.,Sievert, V.,Buessow, K.,Leitner, D.,Labudde, D.,Ball, L.J.,Oschkinat, H. (deposition date: 2004-03-23, release date: 2004-11-09, Last modification date: 2024-05-22)

Primary citation

Soukenik, M.,Diehl, A.,Leidert, M.,Sievert, V.,Buessow, K.,Leitner, D.,Labudde, D.,Ball, L.J.,Lechner, A.,Nagler, D.K.,Oschkinat, H.
The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L
FEBS Lett., 576:358-362, 2004

PubMed Abstract: The 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.

PubMed: 15498563
DOI: 10.1016/j.febslet.2004.09.037

Experimental method

SOLUTION NMR