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PDBsum entry 2ckn

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Transferase PDB id
2ckn
Contents
Protein chain
95 a.a.

References listed in PDB file
Key reference
Title Nmr structure of the first ig module of mouse fgfr1.
Authors V.V.Kiselyov, E.Bock, V.Berezin, F.M.Poulsen.
Ref. Protein Sci, 2006, 15, 1512-1515. [DOI no: 10.1110/ps.062207906]
PubMed id 16731982
Abstract
Fibroblast growth factor (FGF) receptors (FGFRs) regulate a multitude of cellular processes during embryogenesis and in the adult. The extracellular part of the prototypical FGFR consists of three Ig modules (Ig1 - Ig3), in which Ig2 and Ig3 determine affinity and specificity for FGF and heparin, while the Ig1 module is thought to have a regulatory function. The crystal structures of the Ig2 and Ig3 modules alone and in complex with FGF have previously been reported. The structure of the Ig1 module is unknown, and very little is known about the structural determinants for the regulatory function of this module. We describe here the NMR structure of the Ig1 module of mouse FGFR1. The three-dimensional fold of the module belongs to the intermediate Ig subgroup and can be described as a beta-barrel consisting of two beta-sheets. One sheet is formed by A', G, F, C, and C', and the other by A, B, B', E, and D beta-strands. The overall strand topology of the Ig1 module is similar to that of the Ig2 and Ig3 modules. However, the A/A' loop of the Ig1 module is much longer than that of the Ig2 and Ig3 modules. It contains eight extra residues compared to the Ig3 module, and five extra residues compared to Ig2.
Figure 1.
Structure of the FGFR1 Ig1 module. Stereo view of an overlay of the backbone atoms of 20 superimposed structures of the Ig1 module.
Figure 2.
Comparison of the secondary structures of the Ig1 and Ig3 modules of FGFR. (A) Ribbon representation of the structure of the Ig1 module. (B) Comparison of the structures of the A/A[prime prime or minute] loop region of the Ig1 and Ig3 modules.
The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 1512-1515) copyright 2006.
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