1dot: Difference between revisions

Revision as of 23:23, 30 June 2008

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File:1dot.png

Template:STRUCTURE 1dot

CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTIONCRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 15299626

About this StructureAbout this Structure

1DOT is a Single protein structure of sequence from Anas platyrhynchos. Full crystallographic information is available from OCA.

ReferenceReference

Structure of diferric duck ovotransferrin at 2.35 A resolution., Rawas A, Muirhead H, Williams J, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):631-40. PMID:15299626

Page seeded by OCA on Mon Jun 30 23:23:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION'''
+===CRYSTALLOGRAPHIC STRUCTURE OF DUCK OVOTRANSFERRIN AT 2.3 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The structure of diferric duck ovotransferrin (DOT) has been determined and refined at a resolution of 2.35 A. The DOT structure, which contains two iron binding sites, is similar to the known transferrin and lactoferrin structures. The two iron-binding sites, one in the N-terminal lobe and one in the C-terminal lobe of the molecule, are similar but not identical. The main differences between the three known structures lie in the relative orientations of the N- and C-lobes with respect to each other. In the DOT structure the large aromatic side chain of Phe322 in the N-lobe packs against the conserved residue Gly387 in the C-lobe. This interaction is at the centre of the interface between the two lobes and could play a crucial role in determining their relative orientation. Other differences between the structures occur in the surface loops and in the peptide connecting the two lobes. The final crystallographic model consists of 5309 protein atoms (686 residues), two Fe(3+) ions, two (bi)carbonate ions and three carbohydrate moities. 318 water molecules have been added to the model. The final R factor is 0.22 for 25 400 observed reflections between 10 and 2.35 A resolution.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299626}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299626 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299626}}
 ==About this Structure==
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 [[Category: Rawas, A.]]
 [[Category: Iron transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:05:46 2008''
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