1BEB
BOVINE BETA-LACTOGLOBULIN, LATTICE X
Summary for 1BEB
Entry DOI | 10.2210/pdb1beb/pdb |
Descriptor | BETA-LACTOGLOBULIN, SULFATE ION (3 entities in total) |
Functional Keywords | lipocalin, milk whey protein, bovine, retinol-binding |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 2 |
Total formula weight | 36754.52 |
Authors | Brownlow, S.,Morais-Cabral, J.H.,Sawyer, L. (deposition date: 1996-12-20, release date: 1997-05-15, Last modification date: 2024-10-09) |
Primary citation | Brownlow, S.,Morais Cabral, J.H.,Cooper, R.,Flower, D.R.,Yewdall, S.J.,Polikarpov, I.,North, A.C.,Sawyer, L. Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin. Structure, 5:481-495, 1997 Cited by PubMed Abstract: beta-Lactoglobulin (beta-Lg) is the major whey protein in the milk of ruminants and many other mammals. Its function is not known, but it undergoes at least two pH-dependent conformational changes which may be important. Bovine beta-Lg crystallizes in several different lattices, and medium-resolution structures of orthorhombic lattice Y and trigonal lattice Z have been published. Triclinic lattice X and lattice Z crystals grow at pH values either side of the pH at which one of the pH-induced conformational changes occurs. A full understanding of the structure is needed to help explain both the conformational changes and the different denaturation behaviour of the genetic variants. PubMed: 9115437DOI: 10.1016/S0969-2126(97)00205-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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