Motion in Cystatin [cystatin]

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Classification Known Fragment Motion, Hinge Mechanism [F-h-2]

Structures
1A67 NMR (chicken) [ PartsList ]
1CEW X-ray (chicken) [ PartsList ]
1G96 Human dimer

Description
Comparison of X-ray and NMR structure determinations shows that an 18 residue segment has changed from alpha-helical (X-ray) to beta-strand conformation (NMR).
Additionally, the dimerized form of human cystatin has undergone domain swapping.

Particular values describing motion
Experimental Methods = xn (Traditional X-ray and NMR)
Creation Date = 19970822
Modification Date = 19970822

References
R A Engh, T Dieckmann, W Bode, E A Auerswald, V Turk, R Huber and H Oschkinat (1993). Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy. J Mol Biol. 234: 1060-1069. [Medline info for 94087720]
Janowski R, Kozak M, Jankowska E, Grzonka Z, Grubb A, Abrahamson M, Jaskolski M. (2001) Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat Struct Biol. 8:316-20. [Medline info for 11276250]

GO terms associated with structures
Molecular functioncysteine protease inhibitor activity

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Cystatin 1cew [ I ] 1a67 [ A ] 108

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
592045-21676 Cystatin domain swapping (chicken --> hu 1cew [ I ] 1g96 [ A ] 120


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