| Autor: |
Gooley PR; Department of Biochemistry, Merck Research Laboratories, Rahway, NJ 07065, USA., O'Connell JF, Marcy AI, Cuca GC, Axel MG, Caldwell CG, Hagmann WK, Becker JW |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular NMR [J Biomol NMR] 1996 Jan; Vol. 7 (1), pp. 8-28. |
| DOI: |
10.1007/BF00190453 |
| Abstrakt: |
Stromelysin-1 is a matrix metalloprotease that has been implicated in a number of degenerative diseases. Here we present the refined NMR solution structure of the catalytic domain of stromelysin-1 complexed with a small inhibitor and compare it to the X-ray crystal structure of the same complex. The structures are similar in global fold and show an unusual bottomless S1' subsite. There are differences, however, in the least well defined regions, Phe83-Ile89, His224-Phe232 and Pro249- Pro250, reflecting the lack of NOE data and large B-factors. The region His224-Phe232 contains residues of the S1' subsite and, consequently, small differences are observed in this subsite. Hydrogen-bond data show that, in contrast to the crystal structure, the solution structure lacks a hydrogen bond between the amide of Tyr223 and the carbonyl of the P3' residue. Analysis of bound water shows two tightly bound water molecules both in the solution and the crystal structure; neither of these waters are in the inhibitor binding site. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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