2bjj: Difference between revisions
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==Overview== | ==Overview== | ||
Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the, host defence against infection and excessive inflammation. As the, availability of (human milk-derived) natural hLF is limited, alternative, means of production of this biopharmaceutical are extensively researched., Here we report the crystal structure of recombinant hLF (rhLF) expressed, in the milk of transgenic cows at a resolution of 2.4 A. To our knowledge, the first reported structure of a recombinant protein produced in milk of, transgenic livestock. Even though rhLF contains oligomannose- and, hybrid-type N-linked glycans next to complex-type glycans, which are the, only glycans found on natural hLF, the structures are identical within the, experimental error (r.m.s. deviation of only 0.28 A for the main-chain, atoms). Of the differences in polymorphic amino acids between the natural, and rhLF variant used, only the side-chain of Asp561 could be modeled into, the rhLF electron density map. Taken together, the results confirm the, structural integrity of the rhLF variant used in this study. It also, confirms the validity of the transgenic cow mammary gland as a vehicle to, produce recombinant human proteins. | Human lactoferrin (hLF) is an iron-binding glycoprotein involved in the, host defence against infection and excessive inflammation. As the, availability of (human milk-derived) natural hLF is limited, alternative, means of production of this biopharmaceutical are extensively researched., Here we report the crystal structure of recombinant hLF (rhLF) expressed, in the milk of transgenic cows at a resolution of 2.4 A. To our knowledge, the first reported structure of a recombinant protein produced in milk of, transgenic livestock. Even though rhLF contains oligomannose- and, hybrid-type N-linked glycans next to complex-type glycans, which are the, only glycans found on natural hLF, the structures are identical within the, experimental error (r.m.s. deviation of only 0.28 A for the main-chain, atoms). Of the differences in polymorphic amino acids between the natural, and rhLF variant used, only the side-chain of Asp561 could be modeled into, the rhLF electron density map. Taken together, the results confirm the, structural integrity of the rhLF variant used in this study. It also, confirms the validity of the transgenic cow mammary gland as a vehicle to, produce recombinant human proteins. | ||
==Disease== | |||
Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602121 602121]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: transgenic cows]] | [[Category: transgenic cows]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:03:21 2007'' | ||
