1b7z: Difference between revisions

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[[Image:1b7z.png|left|200px]]

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~~'''~~STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM~~'''~~

===STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM===

~~==Overview==~~

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~~Lactoferrin binds two Fe(3+) and two CO(2~~-)(3) ions with high affinity. It can also bind other metal ions and anions. In order to determine the perturbations in the environments of the binding sites in the N and C lobes and elsewhere in the protein, the crystal structure of oxalate-~~substituted diferric mare lactoferrin has been determined at 2.7 A resolution.~~ The ~~final model has a crystallographic R factor of 21.3% for all data in~~ the ~~resolution range 17.0-2.7 A. The substitution of an oxalate anion does not perturb~~ the ~~overall structure of the protein, but produces several significant changes~~ at ~~the metal-binding and anion-binding sites~~. ~~The binding of the oxalate anion is symmetrical in both the N and C lobes, unlike in diferric dioxalate human lactoferrin~~, where the ~~oxalate anion binds the metal ion symmetrically in the C lobe and asymmetrically in the N lobe~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10531474}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10531474 is the PubMed ID number.

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==About this Structure==

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[[Category: Lactoferrin]]

[[Category: Metal binding site]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:11:17 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:31:26 2008''

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-[[Image:1b7z.jpg|left|200px]]
+{{Seed}}
+[[Image:1b7z.png|left|200px]]
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 {{STRUCTURE_1b7z|  PDB=1b7z  |  SCENE=  }}
-'''STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM'''
+===STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM===
-==Overview==
+<!--
-Lactoferrin binds two Fe(3+) and two CO(2-)(3) ions with high affinity. It can also bind other metal ions and anions. In order to determine the perturbations in the environments of the binding sites in the N and C lobes and elsewhere in the protein, the crystal structure of oxalate-substituted diferric mare lactoferrin has been determined at 2.7 A resolution. The final model has a crystallographic R factor of 21.3% for all data in the resolution range 17.0-2.7 A. The substitution of an oxalate anion does not perturb the overall structure of the protein, but produces several significant changes at the metal-binding and anion-binding sites. The binding of the oxalate anion is symmetrical in both the N and C lobes, unlike in diferric dioxalate human lactoferrin, where the oxalate anion binds the metal ion symmetrically in the C lobe and asymmetrically in the N lobe.
+The line below this paragraph, {{ABSTRACT_PUBMED_10531474}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10531474 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10531474}}
 ==About this Structure==
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 [[Category: Lactoferrin]]
 [[Category: Metal binding site]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:11:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:31:26 2008''