3D95

Crystal Structure of the R132K:Y134F:R111L:L121E:T54V Mutant of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.20 Angstroms Resolution

Summary for 3D95

• Entry DOI: 10.2210/pdb3d95/pdb
• Related: 2fr3 2frs 2fs6 2fs7 2g78 2g79 2g7b 3D96 3D97 3cwk
• Descriptor: Cellular retinoic acid-binding protein 2 (2 entities in total)
• Functional Keywords: crabpii, retinoic acid, retinoids, beta barrel, high resolution, mutant, cytoplasm, nucleus, retinol-binding, transport, vitamin a, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 2
• Total formula weight: 31015.47

Authors

Vaezeslami, S.,Geiger, J.H. (deposition date: 2008-05-26, release date: 2008-07-22, Last modification date: 2024-02-21)

Primary citation

Vaezeslami, S.,Jia, X.,Vasileiou, C.,Borhan, B.,Geiger, J.H.
Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding.
Acta Crystallogr.,Sect.D, 64:1228-1239, 2008

PubMed 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.

PubMed: 19018099
DOI: 10.1107/S0907444908032216

Experimental method

X-RAY DIFFRACTION (1.2 Å)