1evt

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[[Image:1evt.gif|left|200px]]
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{{STRUCTURE_1evt| PDB=1evt | SCENE= }}
{{STRUCTURE_1evt| PDB=1evt | SCENE= }}
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'''CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)'''
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===CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 10830168 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10830168}}
==About this Structure==
==About this Structure==
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[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
[[Category: B-trefoil fold]]
[[Category: B-trefoil fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:34:44 2008''
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Revision as of 23:06, 30 June 2008

Template:STRUCTURE 1evt

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

Template:ABSTRACT PUBMED 10830168

About this Structure

1EVT is a Protein complex structure of sequences from Homo sapiens. 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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