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Ovine ?-lactoglobulin at atomic resolution.


ABSTRACT: The crystal structure of the triclinic form of the milk protein ?-lactoglobulin from sheep (Ovis aries) at 1.1?Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.

SUBMITTER: Kontopidis G 

PROVIDER: S-EPMC4231851 | BioStudies | 2014-01-01

REPOSITORIES: biostudies

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