1evt

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(New page: 200px<br /> <applet load="1evt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evt, resolution 2.80&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1evt.gif|left|200px]]<br />
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[[Image:1evt.gif|left|200px]]<br /><applet load="1evt" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1evt" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1evt, resolution 2.80&Aring;" />
caption="1evt, resolution 2.80&Aring;" />
'''CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)'''<br />
'''CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)'''<br />
==Overview==
==Overview==
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To elucidate the structural determinants governing specificity in, fibroblast growth factor (FGF) signaling, we have determined the crystal, structures of FGF1 and FGF2 complexed with the ligand binding domains, (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1), and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between, D2-D3) interfaces define a general binding site for all FGF-FGFR, complexes. Specificity is achieved through interactions between the, N-terminal and central regions of FGFs and two loop regions in D3 that are, subject to alternative splicing. These structures provide a molecular, basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR, specificity through primary sequence variations and alternative splicing.
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To elucidate the structural determinants governing specificity in fibroblast growth factor (FGF) signaling, we have determined the crystal structures of FGF1 and FGF2 complexed with the ligand binding domains (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1) and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between D2-D3) interfaces define a general binding site for all FGF-FGFR complexes. Specificity is achieved through interactions between the N-terminal and central regions of FGFs and two loop regions in D3 that are subject to alternative splicing. These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1EVT 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVT OCA].
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1EVT 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVT OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Hubbard, S.R.]]
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[[Category: Hubbard, S R.]]
[[Category: Mohammadi, M.]]
[[Category: Mohammadi, M.]]
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[[Category: Plotnikov, A.N.]]
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[[Category: Plotnikov, A N.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: immunoglobulin (ig) like domains belonging to the i-set subgroup within ig-like domains]]
[[Category: immunoglobulin (ig) like domains belonging to the i-set subgroup within ig-like domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:47:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:02 2008''

Revision as of 10:32, 21 February 2008


1evt, resolution 2.80Å

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CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)

Contents

Overview

To elucidate the structural determinants governing specificity in fibroblast growth factor (FGF) signaling, we have determined the crystal structures of FGF1 and FGF2 complexed with the ligand binding domains (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1) and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between D2-D3) interfaces define a general binding site for all FGF-FGFR complexes. Specificity is achieved through interactions between the N-terminal and central regions of FGFs and two loop regions in D3 that are subject to alternative splicing. These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing.

Disease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], Atopic dermatitis, susceptibility to OMIM:[135940], Ichthyosis vulgaris OMIM:[135940], Jackson-Weiss syndrome OMIM:[136350], Kallmann syndrome 2 OMIM:[136350], LADD syndrome OMIM:[602115], Pfeiffer syndrome OMIM:[136350]

About this Structure

1EVT is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity., Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M, Cell. 2000 May 12;101(4):413-24. PMID:10830168

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