2ckn

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(New page: 200px<br /><applet load="2ckn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ckn" /> '''NMR STRUCTURE OF THE FIRST IG MODULE OF MOUS...)
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'''NMR STRUCTURE OF THE FIRST IG MODULE OF MOUSE FGFR1'''<br />
'''NMR STRUCTURE OF THE FIRST IG MODULE OF MOUSE FGFR1'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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2CKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CKN OCA].
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2CKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKN OCA].
==Reference==
==Reference==
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[[Category: Berezin, V.]]
[[Category: Berezin, V.]]
[[Category: Bock, E.]]
[[Category: Bock, E.]]
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[[Category: Kiselyov, V.V.]]
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[[Category: Kiselyov, V V.]]
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[[Category: Poulsen, F.M.]]
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[[Category: Poulsen, F M.]]
[[Category: alternatice splicing]]
[[Category: alternatice splicing]]
[[Category: atp-binding]]
[[Category: atp-binding]]
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[[Category: tyrosine-protein kinase]]
[[Category: tyrosine-protein kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:09:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:41 2008''

Revision as of 14:49, 21 February 2008


2ckn

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NMR STRUCTURE OF THE FIRST IG MODULE OF MOUSE FGFR1

Overview

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.

About this Structure

2CKN is a Single protein structure of sequence from [1]. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.

Reference

NMR structure of the first Ig module of mouse FGFR1., Kiselyov VV, Bock E, Berezin V, Poulsen FM, Protein Sci. 2006 Jun;15(6):1512-5. PMID:16731982

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