1mox: Difference between revisions

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New page: left|200px<br /> <applet load="1mox" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mox, resolution 2.5Å" /> '''Crystal Structure of...
 
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[[Image:1mox.gif|left|200px]]<br />
[[Image:1mox.gif|left|200px]]<br /><applet load="1mox" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mox" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mox, resolution 2.5&Aring;" />
caption="1mox, resolution 2.5&Aring;" />
'''Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha'''<br />
'''Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha'''<br />


==Overview==
==Overview==
We report the crystal structure, at 2.5 A resolution, of a truncated human, EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2, domains of EGFR, making many main chain contacts with L1 and interacting, with L2 via key conserved residues. The results indicate how EGFR family, members can bind a family of highly variable ligands. In the 2:2, TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor, molecule. There are two types of dimers in the asymmetric unit: a, head-to-head dimer involving contacts between the L1 and L2 domains and a, back-to-back dimer dominated by interactions between the CR1 domains of, each receptor. Based on sequence conservation, buried surface area, and, mutagenesis experiments, the back-to-back dimer is favored to be, biologically relevant.
We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues. The results indicate how EGFR family members can bind a family of highly variable ligands. In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule. There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor. Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1MOX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, PT, CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MOX OCA].  
1MOX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PT:'>PT</scene>, <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOX OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Adams, T.E.]]
[[Category: Adams, T E.]]
[[Category: Burgess, A.W.]]
[[Category: Burgess, A W.]]
[[Category: Elleman, T.C.]]
[[Category: Elleman, T C.]]
[[Category: Frenkel, M.J.]]
[[Category: Frenkel, M J.]]
[[Category: Garrett, T.P.J.]]
[[Category: Garrett, T P.J.]]
[[Category: Hoyne, P.A.]]
[[Category: Hoyne, P A.]]
[[Category: Jorissen, R.N.]]
[[Category: Jorissen, R N.]]
[[Category: Lou, M.]]
[[Category: Lou, M.]]
[[Category: Lovrecz, G.O.]]
[[Category: Lovrecz, G O.]]
[[Category: McKern, N.M.]]
[[Category: McKern, N M.]]
[[Category: Nice, E.C.]]
[[Category: Nice, E C.]]
[[Category: Walker, F.]]
[[Category: Walker, F.]]
[[Category: Ward, C.W.]]
[[Category: Ward, C W.]]
[[Category: Zhu, H.J.]]
[[Category: Zhu, H J.]]
[[Category: CD]]
[[Category: CD]]
[[Category: CL]]
[[Category: CL]]
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[[Category: receptor]]
[[Category: receptor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:13:28 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:33 2008''