1cvs: Difference between revisions

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|PDB= 1cvs |SIZE=350|CAPTION= <scene name='initialview01'>1cvs</scene>, resolution 2.80&Aring;
|PDB= 1cvs |SIZE=350|CAPTION= <scene name='initialview01'>1cvs</scene>, resolution 2.80&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvs OCA], [http://www.ebi.ac.uk/pdbsum/1cvs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvs RCSB]</span>
}}
}}


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==Overview==
==Overview==
The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.
The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.
==Disease==
Known diseases associated with this structure: Atopic dermatitis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=135940 135940]], Hypophosphatemic rickets, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]], Ichthyosis vulgaris OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=135940 135940]], Jackson-Weiss syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]], Kallmann syndrome 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]], Osteomalacia, tumor-induced OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]], Pfeiffer syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]]


==About this Structure==
==About this Structure==
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[[Category: Plotnikov, A N.]]
[[Category: Plotnikov, A N.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
[[Category: SO4]]
[[Category: dimerization]]
[[Category: dimerization]]
[[Category: fgf]]
[[Category: fgf]]
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[[Category: signal transduction]]
[[Category: signal transduction]]


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