1qo6
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1qo6.gif|left|200px]] | [[Image:1qo6.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1qo6", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1qo6| PDB=1qo6 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING DOMAIN OF FIBRONECTIN''' | '''SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING DOMAIN OF FIBRONECTIN''' | ||
| Line 29: | Line 26: | ||
[[Category: Pickford, A R.]] | [[Category: Pickford, A R.]] | ||
[[Category: Potts, J R.]] | [[Category: Potts, J R.]] | ||
| - | [[Category: | + | [[Category: Fibronectin module pair]] |
| - | [[Category: | + | [[Category: Gelatin-binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:30:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:30, 3 May 2008
SOLUTION STRUCTURE OF A PAIR OF MODULES FROM THE GELATIN-BINDING DOMAIN OF FIBRONECTIN
Overview
BACKGROUND: Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen. RESULTS: The solution structure of the 101-residue 6F1 1F2 module pair, which has a weak affinity for gelatin, has been determined by multidimensional NMR spectroscopy. The tertiary structures determined for each module conform to the F1 and F2 consensus folds established previously. The experimental data suggest that the two modules interact via a small hydrophobic interface but may not be tightly associated. Near-random-coil 1H NMR chemical shifts and fast dynamics for backbone atoms in the linker indicate that this region is unlikely to be involved in the overall stabilisation of the module pair. CONCLUSIONS: The modules in the 6F1 1F2 module pair interact with each other via a flexible linker and a hydrophobic patch, which lies on the opposite side of the 1F2 module to the putative collagen-binding site. The intermodule interaction is relatively weak and transient.
About this Structure
1QO6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a pair of modules from the gelatin-binding domain of fibronectin., Bocquier AA, Potts JR, Pickford AR, Campbell ID, Structure. 1999 Dec 15;7(12):1451-60. PMID:10647176 Page seeded by OCA on Sat May 3 06:30:34 2008
