1D4N

HUMAN SERUM TRANSFERRIN

Summary for 1D4N

• Entry DOI: 10.2210/pdb1d4n/pdb
• Related: 1A8E 1A8F 1D3K
• Descriptor: TRANSFERRIN, CARBONATE ION, FE (III) ION, ... (4 entities in total)
• Functional Keywords: iron transport, glycoprotein, transferrin, n-lobe, iron-release, carbonate, metal transport
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02787
• Total number of polymer chains: 1
• Total formula weight: 36515.23

Authors

Yang, H.-W.,MacGillivray, R.T.A.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.,Woodworth, R.C.,Murphy, M.E.P. (deposition date: 1999-10-04, release date: 2000-03-01, Last modification date: 2024-10-30)

Primary citation

Yang, A.H.,MacGillivray, R.T.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.B.,Woodworth, R.C.,Murphy, M.E.
Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron.
Protein Sci., 9:49-52, 2000

PubMed Abstract: The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.

PubMed: 10739246

Experimental method

X-RAY DIFFRACTION (2 Å)