Motion in Cystatin [cystatin]
[ jump to morphs ]
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 function cysteine protease inhibitor activity
Morphs
[ show all images ]
Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu