1s78

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(New page: 200px<br /> <applet load="1s78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s78, resolution 3.25&Aring;" /> '''Insights into ErbB ...)
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'''Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex'''<br />
'''Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex'''<br />
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==About this Structure==
==About this Structure==
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1S78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1S78 OCA].
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1S78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1S78 OCA].
==Reference==
==Reference==
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[[Category: receptor-antibody complex]]
[[Category: receptor-antibody complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:10:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:52:48 2008''

Revision as of 14:52, 15 February 2008


1s78, resolution 3.25Å

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Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex

Contents

Overview

We have determined the 3.2 A X-ray crystal structure of the extracellular, domain of the human epidermal growth factor receptor 2 (ErbB2 or HER2) in, a complex with the antigen binding fragment of pertuzumab, an anti-ErbB2, monoclonal antibody also known as 2C4 or Omnitarg. Pertuzumab binds to, ErbB2 near the center of domain II, sterically blocking a binding pocket, necessary for receptor dimerization and signaling. The ErbB2-pertuzumab, structure, combined with earlier mutagenesis data, defines the pertuzumab, residues essential for ErbB2 interaction. To analyze the ErbB2 side of the, interface, we have mutated a number of residues contacting pertuzumab and, examined the effects of these mutations on pertuzumab binding and, ErbB2-ErbB3 heterodimerization. We have also shown that conserved residues, previously shown to be necessary for EGF receptor homodimerization may be, dispensible for ErbB2-ErbB3 heterodimerization.

Disease

Known diseases associated with this structure: Adenocarcinoma of lung, somatic OMIM:[164870], Gastric cancer, somatic OMIM:[164870], Glioblastoma, somatic OMIM:[164870], Ovarian cancer, somatic, OMIM:[164870], Sialidosis, type I OMIM:[608272], Sialidosis, type II OMIM:[608272]

About this Structure

1S78 is a Single protein structure of sequence from Homo sapiens and Mus musculus with as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex., Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sliwkowski MX, Cancer Cell. 2004 Apr;5(4):317-28. PMID:15093539

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