1ivo
From Proteopedia
(New page: 200px<br /> <applet load="1ivo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ivo, resolution 3.30Å" /> '''Crystal Structure o...) |
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| - | [[Image:1ivo.gif|left|200px]]<br /> | + | [[Image:1ivo.gif|left|200px]]<br /><applet load="1ivo" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ivo" size=" | + | |
caption="1ivo, resolution 3.30Å" /> | caption="1ivo, resolution 3.30Å" /> | ||
'''Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.'''<br /> | '''Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Epidermal growth factor (EGF) regulates cell proliferation and | + | Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution. EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III. The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other. The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis. |
==Disease== | ==Disease== | ||
| - | Known diseases associated with this structure: Adenocarcinoma of lung, response to tyrosine kinase inhibitor in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]], Nonsmall cell lung cancer, response to tyrosine kinase inhibitor in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]], Nonsmall cell lung cancer, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]] | + | Known diseases associated with this structure: Adenocarcinoma of lung, response to tyrosine kinase inhibitor in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]], Hypomagnesemia 4, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131530 131530]], Nonsmall cell lung cancer, response to tyrosine kinase inhibitor in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]], Nonsmall cell lung cancer, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=131550 131550]] |
==About this Structure== | ==About this Structure== | ||
| - | 1IVO 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 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:// | + | 1IVO 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> 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=1IVO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fukai, S.]] | [[Category: Fukai, S.]] | ||
[[Category: Ishitani, R.]] | [[Category: Ishitani, R.]] | ||
| - | [[Category: Kim, J | + | [[Category: Kim, J H.]] |
[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
[[Category: Ogiso, H.]] | [[Category: Ogiso, H.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Saito, K.]] | [[Category: Saito, K.]] | ||
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:07 2008'' |
Revision as of 11:16, 21 February 2008
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Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.
Contents |
Overview
Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution. EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III. The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other. The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.
Disease
Known diseases associated with this structure: Adenocarcinoma of lung, response to tyrosine kinase inhibitor in OMIM:[131550], Hypomagnesemia 4, renal OMIM:[131530], Nonsmall cell lung cancer, response to tyrosine kinase inhibitor in OMIM:[131550], Nonsmall cell lung cancer, susceptibility to OMIM:[131550]
About this Structure
1IVO is a Protein complex structure of sequences from Homo sapiens 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
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains., Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S, Cell. 2002 Sep 20;110(6):775-87. PMID:12297050
Page seeded by OCA on Thu Feb 21 13:16:07 2008
Categories: Homo sapiens | Protein complex | Transferase | Fukai, S. | Ishitani, R. | Kim, J H. | Nureki, O. | Ogiso, H. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Saito, K. | Shirouzu, M. | Yamanaka, M. | Yokoyama, S. | NAG | Glycoprotein | Receptor | Repeat | Riken structural genomics/proteomics initiative | Rsgi | Signal | Structural genomics | Transmembrane
