Unknown

Dataset Information

0

Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding.

ABSTRACT: The structural integrity of cellular retinoic acid-binding protein II (CRABPII) has been investigated using the crystal structures of CRABPII mutants. The overall fold was well maintained by these CRABPII mutants, each of which carried multiple different mutations. A water-mediated network is found to be present across the large binding cavity, extending from Arg111 deep inside the cavity to the alpha2 helix at its entrance. This chain of interactions acts as a ;pillar' that maintains the integrity of the protein. The disruption of the water network upon loss of Arg111 leads to decreased structural integrity of the protein. A water-mediated network can be re-established by introducing the hydrophilic Glu121 inside the cavity, which results in a rigid protein with the alpha2 helix adopting an altered conformation compared with wild-type CRABPII.

SUBMITTER: Vaezeslami S 

PROVIDER: S-EPMC2631107 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding.

Vaezeslami Soheila S   Jia Xiaofei X   Vasileiou Chrysoula C   Borhan Babak B   Geiger James H JH  

Acta crystallographica. Section D, Biological crystallography 20081118 Pt 12

The structural integrity of cellular retinoic acid-binding protein II (CRABPII) has been investigated using the crystal structures of CRABPII mutants. The overall fold was well maintained by these CRABPII mutants, each of which carried multiple different mutations. A water-mediated network is found to be present across the large binding cavity, extending from Arg111 deep inside the cavity to the alpha2 helix at its entrance. This chain of interactions acts as a ;pillar' that maintains the integr  ...[more]

Similar Datasets

Unknown Role of Structural Features in Oligomerization, Active-Site Integrity and Ligand Binding of Ribose-1,5-Bisphosphate Isomerase.
| S-EPMC6423476 | biostudies-literature
Unknown Site-directed ligand discovery.
| S-EPMC16870 | biostudies-literature
Unknown Site-directed mutants of human RECQ1 reveal functional importance of the zinc binding domain.
| S-EPMC4967042 | biostudies-literature
Unknown Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase.
| S-EPMC6642699 | biostudies-literature
Unknown Nonbinding site-directed mutants of transferrin binding protein B exhibit enhanced immunogenicity and protective capabilities.
| S-EPMC4333475 | biostudies-literature
Unknown Ligand-binding PAS domains in a genomic, cellular, and structural context.
| S-EPMC3298442 | biostudies-literature
Unknown The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
| S-EPMC2519384 | biostudies-literature
Unknown Structural insights into binding-site access and ligand recognition by human ABCB1.
| S-EPMC11833089 | biostudies-literature
Unknown Structural insight into binding site access and ligand recognition by human ABCB1.
| S-EPMC11343101 | biostudies-literature
Unknown Transporter-to-trap conversion: a disulfide bond formation in cellular retinoic acid binding protein I mutant triggered by retinoic acid binding irreversibly locks the ligand inside the protein.
| S-EPMC2519245 | biostudies-literature