From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1cb6.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1cb6.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1cb6| PDB=1cb6 | SCENE= }} | | {{STRUCTURE_1cb6| PDB=1cb6 | SCENE= }} |
| | | | |
| - | '''STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.'''
| + | ===STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The three-dimensional structure of a form of human apolactoferrin, in which one lobe (the N-lobe) has an open conformation and the other lobe (the C-lobe) is closed, has been refined at 2.0 A resolution. The refinement, by restrained least-squares methods, used synchrotron radiation X-ray diffraction data combined with a lower resolution diffractometer data set. The final refined model (5346 protein atoms from residues 1-691, two Cl- ions and 363 water molecules) gives a crystallographic R factor of 0.201 (Rfree = 0. 286) for all 51305 reflections in the resolution range 10.0-2.0 A. The conformational change in the N-lobe, which opens up the binding cleft, involves a 54 degrees rotation of the N2 domain relative to the N1 domain. This also results in a small reorientation of the two lobes relative to one another with a further approximately 730 A2 of surface area being buried as the N2 domain contacts the C-lobe and the inter-lobe helix. These new contacts also involve the C-terminal helix and provide a mechanism through which the conformational and iron-binding status of the N-lobe can be signalled to the C-lobe. Surface-area calculations indicate a fine balance between open and closed forms of lactoferrin, which both have essentially the same solvent-accessible surface. Chloride ions are bound in the anion-binding sites of both lobes, emphasizing the functional significance of these sites. The closed configuration of the C-lobe, attributed in part to weak stabilization by crystal packing interactions, has important implications for lactoferrin dynamics. It shows that a stable closed structure, essentially identical to that of the iron-bound form, can be formed in the absence of iron binding.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10089508}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10089508 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10089508}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Conformational change]] | | [[Category: Conformational change]] |
| | [[Category: Iron transport]] | | [[Category: Iron transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:32:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:30:12 2008'' |
Revision as of 17:30, 30 June 2008
Template:STRUCTURE 1cb6
STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.
Template:ABSTRACT PUBMED 10089508
About this Structure
1CB6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change., Jameson GB, Anderson BF, Norris GE, Thomas DH, Baker EN, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1319-35. PMID:10089508
Page seeded by OCA on Mon Jun 30 20:30:12 2008
