1igr: Difference between revisions
New page: left|200px<br /> <applet load="1igr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igr, resolution 2.6Å" /> '''TYPE 1 INSULIN-LIKE ... |
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[[Image:1igr.gif|left|200px]]<br /> | [[Image:1igr.gif|left|200px]]<br /><applet load="1igr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1igr, resolution 2.6Å" /> | caption="1igr, resolution 2.6Å" /> | ||
'''TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)'''<br /> | '''TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)'''<br /> | ||
==Overview== | ==Overview== | ||
The type-1 insulin-like growth-factor receptor (IGF-1R) and insulin | The type-1 insulin-like growth-factor receptor (IGF-1R) and insulin receptor (IR) are closely related members of the tyrosine-kinase receptor superfamily. IR is essential for glucose homeostasis, whereas IGF-1R is involved in both normal growth and development and malignant transformation. Homologues of these receptors are found in animals as simple as cnidarians. The epidermal growth-factor receptor (EGFR) family is closely related to the IR family and has significant sequence identity to the extracellular portion we describe here. We now present the structure of the first three domains of IGF-IR (L1-Cys-rich-L2) determined to 2.6 A resolution. The L domains each consist of a single-stranded right-handed beta-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. Although the fragment (residues 1-462) does not bind ligand, many of the determinants responsible for hormone binding and ligand specificity map to this central site. This structure therefore shows how the IR subfamily might interact with their ligands. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1IGR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and SO4 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:// | 1IGR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</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=1IGR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Bentley, J | [[Category: Bentley, J D.]] | ||
[[Category: Cosgrove, L | [[Category: Cosgrove, L J.]] | ||
[[Category: Elleman, T | [[Category: Elleman, T C.]] | ||
[[Category: Frenkel, M | [[Category: Frenkel, M J.]] | ||
[[Category: Garrett, T | [[Category: Garrett, T P.J.]] | ||
[[Category: Lou, M.]] | [[Category: Lou, M.]] | ||
[[Category: Lovrecz, G | [[Category: Lovrecz, G O.]] | ||
[[Category: Mckern, N | [[Category: Mckern, N M.]] | ||
[[Category: Ward, C | [[Category: Ward, C W.]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: insulin receptor family]] | [[Category: insulin receptor family]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:39 2008'' | ||
Revision as of 14:11, 21 February 2008
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TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)
OverviewOverview
The type-1 insulin-like growth-factor receptor (IGF-1R) and insulin receptor (IR) are closely related members of the tyrosine-kinase receptor superfamily. IR is essential for glucose homeostasis, whereas IGF-1R is involved in both normal growth and development and malignant transformation. Homologues of these receptors are found in animals as simple as cnidarians. The epidermal growth-factor receptor (EGFR) family is closely related to the IR family and has significant sequence identity to the extracellular portion we describe here. We now present the structure of the first three domains of IGF-IR (L1-Cys-rich-L2) determined to 2.6 A resolution. The L domains each consist of a single-stranded right-handed beta-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. Although the fragment (residues 1-462) does not bind ligand, many of the determinants responsible for hormone binding and ligand specificity map to this central site. This structure therefore shows how the IR subfamily might interact with their ligands.
DiseaseDisease
Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[147370]
About this StructureAbout this Structure
1IGR is a Single protein structure of sequence from Homo sapiens with and as ligands. 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.
ReferenceReference
Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor., Garrett TP, McKern NM, Lou M, Frenkel MJ, Bentley JD, Lovrecz GO, Elleman TC, Cosgrove LJ, Ward CW, Nature. 1998 Jul 23;394(6691):395-9. PMID:9690478
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