1biy: Difference between revisions

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[[Image:1biy.~~jpg~~|left|200px]]

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

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~~'''~~STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN~~'''~~

===STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN===

~~==Overview==~~

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~~The three~~-dimensional structure of diferric buffalo lactoferrin has been determined at 3.3 A resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-~~PLOR).~~ The ~~final model comprises 5316 protein atoms for all 689 residues~~, ~~two Fe(3+) and two CO(3)(2-) ions. The final R factor was 21.8% for 11 711 reflections in~~ the ~~resolution range 17.0-3.3 A. The folding of buffalo lactoferrin is essentially similar~~ to ~~that of~~ the ~~other members of the transferrin family~~. ~~The significant differences are found in the dimensions of the binding cleft and the interlobe orientation~~. ~~The interlobe interactions are predominantly hydrophobic in nature~~, ~~thus facilitating~~ the ~~sliding of two lobes owing to external forces. The interdomain interactions are comparable in the N and C lobes~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10818344}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10818344 is the PubMed ID number.

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==About this Structure==

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[[Category: Lactoferrin]]

[[Category: Structure]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:34:29 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:14:18 2008''

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-[[Image:1biy.jpg|left|200px]]
+{{Seed}}
+[[Image:1biy.png|left|200px]]
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 {{STRUCTURE_1biy|  PDB=1biy  |  SCENE=  }}
-'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN'''
+===STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN===
-==Overview==
+<!--
-The three-dimensional structure of diferric buffalo lactoferrin has been determined at 3.3 A resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-PLOR). The final model comprises 5316 protein atoms for all 689 residues, two Fe(3+) and two CO(3)(2-) ions. The final R factor was 21.8% for 11 711 reflections in the resolution range 17.0-3.3 A. The folding of buffalo lactoferrin is essentially similar to that of the other members of the transferrin family. The significant differences are found in the dimensions of the binding cleft and the interlobe orientation. The interlobe interactions are predominantly hydrophobic in nature, thus facilitating the sliding of two lobes owing to external forces. The interdomain interactions are comparable in the N and C lobes.
+The line below this paragraph, {{ABSTRACT_PUBMED_10818344}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10818344 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10818344}}
 ==About this Structure==
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 [[Category: Lactoferrin]]
 [[Category: Structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:34:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:14:18 2008''