1EV2

CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2)

Summary for 1EV2

• Entry DOI: 10.2210/pdb1ev2/pdb
• Related: 1CVS 1EVT
• Descriptor: PROTEIN (FIBROBLAST GROWTH FACTOR 2), PROTEIN (FIBROBLAST GROWTH FACTOR RECEPTOR 2), SULFATE ION, ... (4 entities in total)
• Functional Keywords: immunoglobulin (ig)like domains belonging to the i-set subgroup within ig-like domains, b-trefoil fold, growth factor-growth factor receptor complex, growth factor/growth factor receptor
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein. Isoform 14: Secreted. Isoform 19: Secreted: P21802
• Total number of polymer chains: 8
• Total formula weight: 159389.34

Authors

Plotnikov, A.N.,Hubbard, S.R.,Schlessinger, J.,Mohammadi, M. (deposition date: 2000-04-19, release date: 2000-05-31, Last modification date: 2024-11-06)

Primary citation

Plotnikov, A.N.,Hubbard, S.R.,Schlessinger, J.,Mohammadi, M.
Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity.
Cell(Cambridge,Mass.), 101:413-424, 2000

PubMed 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.

PubMed: 10830168
DOI: 10.1016/S0092-8674(00)80851-X

Experimental method

X-RAY DIFFRACTION (2.2 Å)