Crystal Structures of Two FGF-FGFR Complexes Reveal the Determinants of Ligand-Receptor Specificity

by: Alexander N Plotnikov, Stevan R Hubbard, Joseph Schlessinger, Moosa Mohammadi

Cell, Vol. 101, No. 4. (12 May 2000), pp. 413-424.

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Abstract

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.

@article{citeulike:2795569, abstract = {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.}, author = {Plotnikov, Alexander N. and Hubbard, Stevan R. and Schlessinger, Joseph and Mohammadi, Moosa }, citeulike-article-id = {2795569}, doi = {10.1016/S0092-8674(00)80851-X}, journal = {Cell}, keywords = {fgf, h}, month = {May}, number = {4}, pages = {413--424}, posted-at = {2008-05-13 17:07:24}, priority = {2}, title = {Crystal Structures of Two FGF-FGFR Complexes Reveal the Determinants of Ligand-Receptor Specificity}, url = {http://dx.doi.org/10.1016/S0092-8674(00)80851-X}, volume = {101}, year = {2000} }

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TY - JOUR ID - citeulike:2795569 L3 - citeulike-article-id:2795569 TI - Crystal Structures of Two FGF-FGFR Complexes Reveal the Determinants of Ligand-Receptor Specificity JF - Cell VL - 101 IS - 4 SP - 413 EP - 424 N2 - 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. KW - fgf KW - h AU - Plotnikov, Alexander AU - Hubbard, Stevan AU - Schlessinger, Joseph AU - Mohammadi, Moosa PY - 2000/05/12/ UR - http://dx.doi.org/10.1016/S0092-8674(00)80851-X ER -

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