Motion in Stromelysin catalytic domain [strlys]

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Classification [F-?-2]

Structures
1CQR
1CAQ

Description
Conformational changes have been detected in X-ray studies of stromelysin bound to various inhibitors.

References
S Pikul, K L McDow Dunham, N G Almstead, B De, M G Natchus, M V Anastasio, S J McPhail, C E Snider, Y O Taiwo, L Chen, C M Dunaway, F Gu, G E Mieling (1999). Design and synthesis of phosphinamide-based hydroxamic acids as inhibitors of matrix metalloproteinases. J Med Chem, 42:87-94 [Medline info for 9888835]
A G Pavlovsky, M G Williams, Q Z Ye, D F Ortwine, C F Purchase, A D White, V Dhanaraj, B D Roth, L L Johnson, D Hupe, C Humblet, T L Blundell (1999). X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity. Protein Sci, 8:1455-62 [Medline info for 10422833]
L Chen, T J Rydel, F Gu, C M Dunaway, S Pikul, K M Dunham, B L Barnett (1999). Crystal structure of the stromelysin catalytic domain at 2.0 A resolution: inhibitor-induced conformational changes. J Mol Biol, 293:545-57 [Medline info for 10543949]

GO terms associated with structures
Molecular functionmetallopeptidase activity, zinc ion binding, metalloendopeptidase activity
Cellular componentextracellular matrix (sensu Metazoa)
Biological processproteolysis and peptidolysis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
stromelysin catalyti 1cqr [ A ] 1caq [ A ] 168



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu