Sulfur in human crystallins.
Molecular models of human gamma-crystallins and the 'alpha-crystallin domain' of human alphaA-crystallin have been built based on available related X-ray crystal structures. The accessibilities of the component cysteine, methionine and tryptophan side chains in the crystallin models have been calculated. The reactivities of these cysteines, which are oxidised in cataract, are assessed based on their known modifications and within the context of their location within the 3D models.
Srikanthan
Durga
D
Department of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
Bateman
Orval A
OA
Purkiss
Andrew G
AG
Slingsby
Christine
C
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D051381:Rats; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013329:Structure-Activity Relationship; D013455:Sulfur / Q000737:chemistry*; D038202:alpha-Crystallin A Chain / Q000737:chemistry; D038222:gamma-Crystallins / Q000737:chemistry
D003459:Crystallins; D038202:alpha-Crystallin A Chain; D038222:gamma-Crystallins; D013455:Sulfur; D003545:Cysteine