1OWW

Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy

Summary for 1OWW

• Entry DOI: 10.2210/pdb1oww/pdb
• Descriptor: Fibronectin first type III module (1 entity in total)
• Functional Keywords: fibronectin type iii module, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 1
• Total formula weight: 10984.31

Authors

Gao, M.,Craig, D.,Lequin, O.,Campbell, I.D.,Vogel, V.,Schulten, K. (deposition date: 2003-03-31, release date: 2003-10-07, Last modification date: 2024-05-01)

Primary citation

Gao, M.,Craig, D.,Lequin, O.,Campbell, I.D.,Vogel, V.,Schulten, K.
Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates
Proc.Natl.Acad.Sci.USA, 100:14784-14789, 2003

PubMed Abstract: Fibronectin (FN) forms fibrillar networks coupling cells to the extracellular matrix. The formation of FN fibrils, fibrillogenesis, is a tightly regulated process involving the exposure of cryptic binding sites in individual FN type III (FN-III) repeats presumably exposed by mechanical tension. The FN-III1 module has been previously proposed to contain such cryptic sites that promote the assembly of extracellular matrix FN fibrils. We have combined NMR and steered molecular dynamics simulations to study the structure and mechanical unfolding pathway of FN-III1. This study finds that FN-III1 consists of a beta-sandwich structure that unfolds to a mechanically stable intermediate about four times the length of the native folded state. Considering previous experimental findings, our studies provide a structural model by which mechanical stretching of FN-III1 may induce fibrillogenesis through this partially unfolded intermediate.

PubMed: 14657397
DOI: 10.1073/pnas.2334390100

Experimental method

SOLUTION NMR