Different segmental flexibility of human serum transferrin and lactoferrin

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

X-ray diffraction studies show that the diferric (holo) forms of human serum transferrin and lactoferrin have almost the same conformation in crystal. In solution, however, the two proteins exhibit different characteristics. The differences are even more pronounced in the apo forms. Small-angle X-ray and neutron scattering data show that lactoferrin is less compact, in apo and holo forms, than the corresponding forms of transferrin in solution. The comparison of primary structures of the two proteins suggests that one of the interdomain hinge regions is significantly longer in lactoferrin than its counterpart in transferrin. The difference in flexibility due to the long hinge region in lactoferrin may be responsible for many of the differences in the physicochemical characteristics of the two proteins.

Original languageEnglish
Pages (from-to)181-184
Number of pages4
JournalArchives of Biochemistry and Biophysics
Volume275
Issue number1
DOIs
Publication statusPublished - Nov 15 1989

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Lactoferrin
Transferrin
Hinges
Serum
Proteins
Neutrons
Neutron scattering
X ray scattering
X-Ray Diffraction
Conformations
Amino Acid Sequence
X-Rays
X ray diffraction
Crystals

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Different segmental flexibility of human serum transferrin and lactoferrin. / Vígh, R.; Cser, L.; Kilár, F.; Simon, I.

In: Archives of Biochemistry and Biophysics, Vol. 275, No. 1, 15.11.1989, p. 181-184.

Research output: Contribution to journalArticle

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