2CG6
Second and third fibronectin type I module pair (crystal form I).
Summary for 2CG6
| Entry DOI | 10.2210/pdb2cg6/pdb |
| Related | 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2FN2 2FNB |
| Descriptor | HUMAN FIBRONECTIN, SULFATE ION (3 entities in total) |
| Functional Keywords | cell adhesion, glycoprotein, heparin-binding, signaling protein, acute phase, alternative splicing, phosphorylation, pyrrolidone carboxylic acid, sulfation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P02751 |
| Total number of polymer chains | 1 |
| Total formula weight | 10216.45 |
| Authors | Rudino-Pinera, E.,Ravelli, R.B.G.,Sheldrick, G.M.,Nanao, M.H.,Werner, J.M.,Schwarz-Linek, U.,Potts, J.R.,Garman, E.F. (deposition date: 2006-02-27, release date: 2007-02-27, Last modification date: 2024-11-13) |
| 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 Cited by 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: 17368672DOI: 10.1016/J.JMB.2007.02.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
Download full validation report
