1djs

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(New page: 200px<br /> <applet load="1djs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1djs, resolution 2.4&Aring;" /> '''LIGAND-BINDING PORTI...)
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'''LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1'''<br />
'''LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1'''<br />
==Overview==
==Overview==
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Fibroblast growth factors (FGFs) effect cellular responses by binding to, FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in, the presence of heparin activates the cytoplasmic receptor tyrosine kinase, through autophosphorylation. We have crystallized a complex between human, FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal, structure, determined by multiwavelength anomalous diffraction analysis of, the selenomethionyl protein, is a dimeric assemblage of 1:1, ligand:receptor complexes. FGF is bound at the junction between the two, domains of one FGFR, and two such units are associated through, receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion, positions appear to mark the course of heparin binding between FGF, molecules through a basic region on receptor D2 domains. This dimeric, assemblage provides a structural mechanism for FGF signal transduction.
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Fibroblast growth factors (FGFs) effect cellular responses by binding to FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in the presence of heparin activates the cytoplasmic receptor tyrosine kinase through autophosphorylation. We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes. FGF is bound at the junction between the two domains of one FGFR, and two such units are associated through receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion positions appear to mark the course of heparin binding between FGF molecules through a basic region on receptor D2 domains. This dimeric assemblage provides a structural mechanism for FGF signal transduction.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1DJS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DJS OCA].
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1DJS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJS OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Transferase]]
[[Category: Transferase]]
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[[Category: Digabriele, A.D.]]
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[[Category: Digabriele, A D.]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Hendrickson, W A.]]
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[[Category: Stauber, D.J.]]
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[[Category: Stauber, D J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: fgf]]
[[Category: fgf]]
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:33:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:17 2008''

Revision as of 10:17, 21 February 2008


1djs, resolution 2.4Å

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LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1

Contents

Overview

Fibroblast growth factors (FGFs) effect cellular responses by binding to FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in the presence of heparin activates the cytoplasmic receptor tyrosine kinase through autophosphorylation. We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal structure, determined by multiwavelength anomalous diffraction analysis of the selenomethionyl protein, is a dimeric assemblage of 1:1 ligand:receptor complexes. FGF is bound at the junction between the two domains of one FGFR, and two such units are associated through receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion positions appear to mark the course of heparin binding between FGF molecules through a basic region on receptor D2 domains. This dimeric assemblage provides a structural mechanism for FGF signal transduction.

Disease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this Structure

1DJS is a Protein complex structure of sequences from Homo sapiens with as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Structural interactions of fibroblast growth factor receptor with its ligands., Stauber DJ, DiGabriele AD, Hendrickson WA, Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):49-54. PMID:10618369

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