The Uteroglobin Fold

: Uteroglobin (UTG) forms a fascinating homodimeric structure that binds small‐ to medium‐sized ligands through an internal hydrophobic cavity, located at the interface between the two monomers. Previous studies have shown that UTG fold is not limited to the UTG/CC10 family, whose sequence/structure...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2000-12, Vol.923 (1), p.90-112
Main Authors: CALLEBAUT, ISABELLE, POUPON, ANNE, BALLY, RÉNÉE, DEMARET, JEAN-PHILIPPE, HOUSSET, DOMINIQUE, DELETTRÉ, JEAN, HOSSENLOPP, PAUL, MORNON, JEAN-PAUL
Format: Article
Language:English
Subjects:
Amino Acid Sequence - physiology
Animals
Cluster Analysis
Humans
Molecular Sequence Data
Protein Structure, Tertiary - physiology
Uteroglobin - chemistry
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Summary:: Uteroglobin (UTG) forms a fascinating homodimeric structure that binds small‐ to medium‐sized ligands through an internal hydrophobic cavity, located at the interface between the two monomers. Previous studies have shown that UTG fold is not limited to the UTG/CC10 family, whose sequence/structure relationships are highlighted here, but can be extended to the cap domain of Xanthobacter autotrophicus haloalkane dehalogenase. We show here that UTG fold is adopted by several other cap domains within the α/β hydrolase family, making it a well‐suited “geode” structure allowing it to sequester various hydrophobic molecules. Additionally, some data about a new crystal form of oxidized rabbit UTG are presented, completing previous structural studies, as well as results from molecular dynamics, suggesting an alternative way for the ligand to reach the internal cavity.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.2000.tb05522.x