2CKU

Solution structure of 2F13F1 from human fibronectin

Summary for 2CKU

• Entry DOI: 10.2210/pdb2cku/pdb
• Related: 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2CG7 2FN2 2FNB
• Descriptor: FIBRONECTIN (1 entity in total)
• Functional Keywords: glycoprotein, cell adhesion, phosphorylation, pyrrolidone carboxylic acid, signaling protein, sulfation, acute phase, fibronectin, module pair, heparin-binding, alternative splicing
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 10120.39

Authors

Werner, J.M.,Potts, J.R. (deposition date: 2006-04-21, release date: 2007-04-03, Last modification date: 2024-10-16)

Primary citation

Rudino-Pinera, E.,Ravelli, R.B.G.,Sheldrick, G.M.,Nanao, M.H.,Korostelev, V.V.,Werner, J.M.,Schwarz-Linek, U.,Potts, J.R.,Garman, E.F.
The Solution and Crystal Structures of a Module Pair from the Staphylococcus Aureus-Binding Site of Human Fibronectin-A Tale with a Twist.
J.Mol.Biol., 368:833-, 2007

PubMed Abstract: An important goal of structural studies of modular proteins is to determine the inter-module orientation, which often influences biological function. The N-terminal domain of human fibronectin (Fn) is composed of a string of five type 1 modules (F1). Despite their small size, to date F1 modules have proved intractable to X-ray structure solution, although there are several NMR structures available. Here, we present the first structures (two X-ray models and an NMR-derived model) of the (2)F1(3)F1 module pair, which forms part of the binding site for Fn-binding proteins from pathogenic bacteria. The crystallographic structure determination was aided by the novel technique of UV radiation damage-induced phasing. The individual module structures are very similar in all three models. In the NMR structure and one of the X-ray structures, a similar but smaller interdomain interface than that observed previously for (4)F1(5)F1 is seen. The other X-ray structure has a different interdomain orientation. This work underlines the benefits of combining X-ray and NMR data in the studies of multi-domain proteins.

PubMed: 17368672
DOI: 10.1016/J.JMB.2007.02.061

Experimental method

SOLUTION NMR