1cn4

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[[Image:1cn4.gif|left|200px]]
[[Image:1cn4.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1cn4| PDB=1cn4 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cn4 OCA], [http://www.ebi.ac.uk/pdbsum/1cn4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cn4 RCSB]</span>
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'''ERYTHROPOIETIN COMPLEXED WITH EXTRACELLULAR DOMAINS OF ERYTHROPOIETIN RECEPTOR'''
'''ERYTHROPOIETIN COMPLEXED WITH EXTRACELLULAR DOMAINS OF ERYTHROPOIETIN RECEPTOR'''
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==About this Structure==
==About this Structure==
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1CN4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1BLW. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CN4 OCA].
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1CN4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1blw 1blw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CN4 OCA].
==Reference==
==Reference==
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[[Category: Reid, S W.]]
[[Category: Reid, S W.]]
[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
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[[Category: cytokine receptor]]
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[[Category: Cytokine receptor]]
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[[Category: haematopoietic cytokine]]
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[[Category: Haematopoietic cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:47 2008''
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Revision as of 09:54, 2 May 2008

Template:STRUCTURE 1cn4

ERYTHROPOIETIN COMPLEXED WITH EXTRACELLULAR DOMAINS OF ERYTHROPOIETIN RECEPTOR


Overview

Human erythropoietin is a haematopoietic cytokine required for the differentiation and proliferation of precursor cells into red blood cells. It activates cells by binding and orientating two cell-surface erythropoietin receptors (EPORs) which trigger an intracellular phosphorylation cascade. The half-maximal response in a cellular proliferation assay is evoked at an erythropoietin concentration of 10 pM, 10(-2) of its Kd value for erythropoietin-EPOR binding site 1 (Kd approximately equal to nM), and 10(-5) of the Kd for erythropoietin-EPOR binding site 2 (Kd approximately equal to 1 microM). Overall half-maximal binding (IC50) of cell-surface receptors is produced with approximately 0.18 nM erythropoietin, indicating that only approximately 6% of the receptors would be bound in the presence of 10 pM erythropoietin. Other effective erythropoietin-mimetic ligands that dimerize receptors can evoke the same cellular responses but much less efficiently, requiring concentrations close to their Kd values (approximately 0.1 microM). The crystal structure of erythropoietin complexed to the extracellular ligand-binding domains of the erythropoietin receptor, determined at 1.9 A from two crystal forms, shows that erythropoietin imposes a unique 120 degrees angular relationship and orientation that is responsible for optimal signalling through intracellular kinase pathways.

About this Structure

1CN4 is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1blw. Full crystallographic information is available from OCA.

Reference

Efficiency of signalling through cytokine receptors depends critically on receptor orientation., Syed RS, Reid SW, Li C, Cheetham JC, Aoki KH, Liu B, Zhan H, Osslund TD, Chirino AJ, Zhang J, Finer-Moore J, Elliott S, Sitney K, Katz BA, Matthews DJ, Wendoloski JJ, Egrie J, Stroud RM, Nature. 1998 Oct 1;395(6701):511-6. PMID:9774108 Page seeded by OCA on Fri May 2 12:54:47 2008

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