Sulfur in human crystallins

Molecular models of human γ-crystallins and the ‘α-crystallin domain’ of human αA-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 re...

Full description

Saved in:
Bibliographic Details
Published inExperimental eye research Vol. 79; no. 6; pp. 823 - 831
Main Authors Srikanthan, Durga, Bateman, Orval A., Purkiss, Andrew G., Slingsby, Christine
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.12.2004
Subjects
alpha-Crystallin A Chain - chemistry
Amino Acid Sequence
Animals
cataract
Cattle
Crystallins - chemistry
Crystallography, X-Ray
cysteine
Cysteine - chemistry
gamma-Crystallins - chemistry
glutathione
homology models
Humans
lens
Models, Molecular
Molecular Sequence Data
oxidation
Oxidation-Reduction
Rats
Sequence Alignment
solvent accessibility
Structural Homology, Protein
Structure-Activity Relationship
sulfinic acid
Sulfur - chemistry
αA-crystallin
βB1-crystallin
γ-crystallins
βB1-crystallin
γ-crystallins
cataract
glutathione
cysteine
homology models
solvent accessibility
αA-crystallin
oxidation
lens
sulfinic acid
Online AccessGet full text

Cover

More Information
Summary:Molecular models of human γ-crystallins and the ‘α-crystallin domain’ of human αA-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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-4835
1096-0007
DOI:10.1016/j.exer.2004.05.009