1igr: Difference between revisions

Revision as of 12:07, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1igr.png

Template:STRUCTURE 1igr

TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)

Template:ABSTRACT PUBMED 9690478

About this StructureAbout this Structure

1IGR is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Tue Jul 1 12:06:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1igr.gif|left|200px]]
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 {{STRUCTURE_1igr|  PDB=1igr  |  SCENE=  }}
-'''TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)'''
+===TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR (DOMAINS 1-3)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9690478}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9690478 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9690478}}
 ==About this Structure==
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 [[Category: Hormone receptor]]
 [[Category: Insulin receptor family]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 12:06:38 2008''