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

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: 9115437
DOI: 10.1016/S0969-2126(97)00205-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)