From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1dsn.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dsn.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1dsn| PDB=1dsn | SCENE= }} | | {{STRUCTURE_1dsn| PDB=1dsn | SCENE= }} |
| | | | |
| - | '''D60S N-TERMINAL LOBE HUMAN LACTOFERRIN'''
| + | ===D60S N-TERMINAL LOBE HUMAN LACTOFERRIN=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of a site-specific mutant of the N-terminal half-molecule of human lactoferrin, Lf(N), in which the iron ligand Asp60 has been mutated to Ser, has been determined at 2.05 A resolution in order to determine the effects of the mutation on iron binding and domain closure. Yellow monoclinic crystals of the D60S mutant, in its iron-bound form, were prepared, and have unit cell dimensions a = 110.2 A, b = 57.0 A, c = 55.2 A, beta = 97.6 degrees, space group C2, with one molecule of 333 residues in the asymmetric unit. The structure was determined by molecular replacement, using the wild-type Lf(N) as search model, and was refined by restrained least-squares methods. The final model, comprising 2451 protein atoms (from residues 2 to 315) one Fe3+ and one CO2-(3), and 107 water molecules, gives an R-factor of 0.175 for all data in the resolution range 20.0 to 2.05 A. The model conforms well with standard geometry, having root-mean-square deviations of 0.014 A and 1.2 degrees from standard bond lengths and angles. The structure of the D60S mutant deviates in two important respects from the parent Lf(N) molecule. At the mutation site the Ser side-chain neither binds to the iron atom nor makes any interdomain contact as the substituted Asp does; instead a water molecule fills the iron coordination site and participates in interdomain hydrogen bonding. The domain closure is also changed, with the D60S mutant having a more closed conformation. Consideration of crystal packing suggests that the altered domain closure is a genuine molecular property but both the iron coordination and interdomain contacts are consistent with weakened iron binding in the mutant. The implications for iron binding in transferrins generally are discussed. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8594202}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8594202 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8594202}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Iron transport]] | | [[Category: Iron transport]] |
| | [[Category: Metal-binding]] | | [[Category: Metal-binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:13:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:33:23 2008'' |
Revision as of 20:33, 30 June 2008
Template:STRUCTURE 1dsn
D60S N-TERMINAL LOBE HUMAN LACTOFERRIN
Template:ABSTRACT PUBMED 8594202
About this Structure
1DSN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin., Faber HR, Bland T, Day CL, Norris GE, Tweedie JW, Baker EN, J Mol Biol. 1996 Feb 23;256(2):352-63. PMID:8594202
Page seeded by OCA on Mon Jun 30 23:33:23 2008
