Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins

Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggests that they may be concerned with...

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Bibliographic Details
Published inInternational journal of biological macromolecules Vol. 11; no. 1; pp. 56 - 58
Main Author North, A.C.T.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.02.1989
Subjects
Amino Acid Sequence
Animals
Beta-lactoglobulin
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Humans
Lactoglobulins - chemistry
Lactoglobulins - metabolism
ligand binding
Ligands
Models, Molecular
Molecular Sequence Data
protein homology
Sequence Homology, Nucleic Acid
ligand binding
Beta-lactoglobulin
protein homology
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Summary:Beta-lactoglobulin has been found to be a member of a super family of proteins that bind specific ligands and which share common features in their amino acid sequences. Here we show that these features are grouped spatially on the surface of the proteins and suggests that they may be concerned with binding to cell-surface receptors.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0141-8130
1879-0003
DOI:10.1016/0141-8130(89)90041-X