1cvs: Difference between revisions
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[[Image:1cvs.jpg|left|200px]] | [[Image:1cvs.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX''' | {{Structure | ||
|PDB= 1cvs |SIZE=350|CAPTION= <scene name='initialview01'>1cvs</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CVS is a [ | 1CVS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVS OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for FGF receptor dimerization and activation., Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M, Cell. 1999 Sep 3;98(5):641-50. PMID:[http:// | Structural basis for FGF receptor dimerization and activation., Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M, Cell. 1999 Sep 3;98(5):641-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10490103 10490103] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:34 2008'' | ||
Revision as of 11:29, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Atopic dermatitis, susceptibility to OMIM:[135940], Hypophosphatemic rickets, autosomal dominant OMIM:[605380], Ichthyosis vulgaris OMIM:[135940], Jackson-Weiss syndrome OMIM:[136350], Kallmann syndrome 2 OMIM:[136350], Osteomalacia, tumor-induced OMIM:[605380], Pfeiffer syndrome OMIM:[136350], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[605380]
About this StructureAbout this Structure
1CVS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for FGF receptor dimerization and activation., Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M, Cell. 1999 Sep 3;98(5):641-50. PMID:10490103
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