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 2.80Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:40, 12 November 2007
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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 SO4 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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