PMID- 10627816
OWN - NLM
STAT- MEDLINE
DCOM- 20000131
LR  - 20091103
IS  - 0950-222X (Print)
IS  - 0950-222X (Linking)
VI  - 13 ( Pt 3b)
DP  - 1999 Jun
TI  - Structure of the crystallins.
PG  - 395-402
AB  - The lens is formed from two protein superfamilies, the alpha- and beta
      gamma-crystallins. Representative three-dimensional structures show they both
      have a basic 2-beta-sheet domain fold, with the beta gamma-domain being made from
      two intercalating Greek keys. X-ray structures of monomeric gamma-crystallins and
      simple oligomeric beta-crystallins show how multiple gene duplications can give
      rise to highly symmetrical assemblies based on paired domains. These protein
      folds have been engineered by directed mutagenesis to investigate the roles of
      the critical region in domain pairing and assembly. Inherited human cataracts
      have been described that are associated with representatives of each of the
      crystallin protein families. Mutations to certain beta- and gamma-crystallin
      genes cause expression of truncated polypeptides that would not be expected to
      fold properly; instead they would randomly aggregate causing light scattering. As
      crystallin proteins are not renewed, age-related cataract is a gradual
      accumulation of small changes to pre-existing normal proteins. The precise sites 
      of post-translational modifications are now being mapped to the various
      crystallins.
FAU - Slingsby, C
AU  - Slingsby C
AD  - Birkbeck College, Department of Crystallography, London, UK.
FAU - Clout, N J
AU  - Clout NJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Eye (Lond)
JT  - Eye (London, England)
JID - 8703986
RN  - 0 (Crystallins)
RN  - 0 (Heat-Shock Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cataract/genetics/*metabolism
MH  - Crystallins/*chemistry/genetics
MH  - Heat-Shock Proteins/chemistry
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Folding
MH  - Protein Structure, Tertiary
RF  - 51
EDAT- 2000/01/11 00:00
MHDA- 2000/01/11 00:01
CRDT- 2000/01/11 00:00
PHST- 2000/01/11 00:00 [pubmed]
PHST- 2000/01/11 00:01 [medline]
PHST- 2000/01/11 00:00 [entrez]
AID - 10.1038/eye.1999.113 [doi]
PST - ppublish
SO  - Eye (Lond). 1999 Jun;13 ( Pt 3b):395-402. doi: 10.1038/eye.1999.113.