1d3k: Difference between revisions

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==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.

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.

==Disease==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Brayer, G.D.]]

[[Category: Brayer, G D.]]

[[Category: Chen, J.]]

[[Category: Luo, Y.]]

[[Category: MacGillivray, R.T.A.]]

[[Category: MacGillivray, R T.A.]]

[[Category: Mason, A.]]

[[Category: Murphy, M.E.P.]]

[[Category: Murphy, M E.P.]]

[[Category: Wang, Y.]]

[[Category: Woodworth, R.C.]]

[[Category: Woodworth, R C.]]

[[Category: Yang, H.W.]]

[[Category: Yang, H W.]]

[[Category: CO3]]

[[Category: FE]]

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[[Category: transferrin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:38:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:42 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Brayer, G.D.]]
+[[Category: Brayer, G D.]]
 [[Category: Chen, J.]]
 [[Category: Luo, Y.]]
-[[Category: MacGillivray, R.T.A.]]
+[[Category: MacGillivray, R T.A.]]
 [[Category: Mason, A.]]
-[[Category: Murphy, M.E.P.]]
+[[Category: Murphy, M E.P.]]
 [[Category: Wang, Y.]]
-[[Category: Woodworth, R.C.]]
+[[Category: Woodworth, R C.]]
-[[Category: Yang, H.W.]]
+[[Category: Yang, H W.]]
 [[Category: CO3]]
 [[Category: FE]]
@@ Line 34: / Line 34: @@
 [[Category: transferrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:38:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:42 2008''