Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.
domain-swapped trimers
human cellular retinol binding protein II
metalloproteins
protein engineering
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
16 11 2020
16 11 2020
Historique:
received:
24
06
2020
revised:
29
06
2020
pubmed:
2
7
2020
medline:
7
7
2021
entrez:
2
7
2020
Statut:
ppublish
Résumé
Domain-swapping is a mechanism for evolving new protein structure from extant scaffolds, and has been an efficient protein-engineering strategy for tailoring functional diversity. However, domain swapping can only be exploited if it can be controlled, especially in cases where various folds can coexist. Herein, we describe the structure of a domain-swapped trimer of the iLBP family member hCRBPII, and suggest a mechanism for domain-swapped trimerization. It is further shown that domain-swapped trimerization can be favored by strategic installation of a disulfide bond, thus demonstrating a strategy for fold control. We further show the domain-swapped trimer to be a useful protein design template by installing a high-affinity metal binding site through the introduction of a single mutation, taking advantage of its threefold symmetry. Together, these studies show how nature can promote oligomerization, stabilize a specific oligomer, and generate new function with minimal changes to the protein sequence.
Identifiants
pubmed: 32608180
doi: 10.1002/cbic.202000405
pmc: PMC8220890
mid: NIHMS1650221
doi:
Substances chimiques
Retinol-Binding Proteins, Cellular
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3192-3196Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM101353
Pays : United States
Informations de copyright
© 2020 Wiley-VCH GmbH.
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