1d4n
From Proteopedia
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'''HUMAN SERUM TRANSFERRIN''' | '''HUMAN SERUM TRANSFERRIN''' | ||
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[[Category: Woodworth, R C.]] | [[Category: Woodworth, R C.]] | ||
[[Category: Yang, H W.]] | [[Category: Yang, H W.]] | ||
- | [[Category: | + | [[Category: Carbonate]] |
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Iron transport]] |
- | [[Category: | + | [[Category: Iron-release]] |
- | [[Category: | + | [[Category: N-lobe]] |
- | [[Category: | + | [[Category: Transferrin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:26:43 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 10:26, 2 May 2008
HUMAN SERUM TRANSFERRIN
Overview
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.
About this Structure
1D4N is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron., Yang AH, MacGillivray RT, Chen J, Luo Y, Wang Y, Brayer GD, Mason AB, Woodworth RC, Murphy ME, Protein Sci. 2000 Jan;9(1):49-52. PMID:10739246 Page seeded by OCA on Fri May 2 13:26:43 2008