1a8f

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File:1a8f.gif


1a8f, resolution 1.80Å

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HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE

OverviewOverview

The N-lobe of human serum transferrin (hTF/2N) has been expressed in baby, hamster kidney cells and crystallized in both orthorhombic (P212121) and, tetragonal (P41212) space groups. Both crystal forms diffract to high, resolution (1.6 and 1.8 A, respectively) and have been solved by molecular, replacement. Subsequent refinement resulted in final models for the, structure of hTF/2N that had crystallographic R-factors of 18.1 and 19.7%, for the two crystal forms, respectively; these models represent the, highest-resolution transferrin structures determined to date. The hTF/2N, polypeptide has a folding pattern similar to those of other transferrins, including the presence of a deep cleft that contains the metal-binding, site. In contrast to other transferrins, both crystal forms of hTF/2N, ... [(full description)]

About this StructureAbout this Structure

1A8F is a [Single protein] structure of sequence from [Homo sapiens] with CO3 and FE as [ligands]. Structure known Active Site: FE. Full crystallographic information is available from [OCA].

ReferenceReference

Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release., MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN, Biochemistry. 1998 Jun 2;37(22):7919-28. PMID:9609685

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