2ahx
From Proteopedia
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|PDB= 2ahx |SIZE=350|CAPTION= <scene name='initialview01'>2ahx</scene>, resolution 2.396Å | |PDB= 2ahx |SIZE=350|CAPTION= <scene name='initialview01'>2ahx</scene>, resolution 2.396Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span> |
|GENE= ERBB4, HER4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ERBB4, HER4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ahx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahx OCA], [http://www.ebi.ac.uk/pdbsum/2ahx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ahx RCSB]</span> | ||
}} | }} | ||
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[[Category: Li, S.]] | [[Category: Li, S.]] | ||
[[Category: Longo, P A.]] | [[Category: Longo, P A.]] | ||
| - | [[Category: | + | [[Category: heparin-binding]] |
| - | [[Category: | + | [[Category: neuregulin]] |
| - | + | [[Category: x-ray crystallography]] | |
| - | + | ||
| - | [[Category: x-ray crystallography | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:55 2008'' |
Revision as of 22:52, 30 March 2008
| |||||||
| , resolution 2.396Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | ERBB4, HER4 (Homo sapiens) | ||||||
| Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of ErbB4/HER4 extracellular domain
Overview
The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4). ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers. We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3. This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation. We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1. These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
About this Structure
2AHX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand., Bouyain S, Longo PA, Li S, Ferguson KM, Leahy DJ, Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15024-9. Epub 2005 Oct 3. PMID:16203964
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