1imx
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1imx.gif|left|200px]] | [[Image:1imx.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1imx", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1imx| PDB=1imx | SCENE= }} | |
- | + | ||
- | | | + | |
- | }} | + | |
'''1.8 Angstrom crystal structure of IGF-1''' | '''1.8 Angstrom crystal structure of IGF-1''' | ||
Line 32: | Line 29: | ||
[[Category: Vajdos, F F.]] | [[Category: Vajdos, F F.]] | ||
[[Category: Vos, A M.de.]] | [[Category: Vos, A M.de.]] | ||
- | [[Category: | + | [[Category: Detergent]] |
- | [[Category: | + | [[Category: Insulin/relaxin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:10:18 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:10, 2 May 2008
1.8 Angstrom crystal structure of IGF-1
Overview
Despite efforts spanning considerably more than a decade, a high-resolution view of the family of proteins known as insulin-like growth factors (IGFs) has remained elusive. IGF-1 consists of three helical segments which are connected by a 12-residue linker known as the C-region. NMR studies of members of this family reveal a dynamic structure with a topology resembling insulin but little structural definition in the C-region. We have crystallized IGF-1 in the presence of the detergent deoxy big CHAPS, and determined its structure at 1.8 A resolution by multiwavelength anomalous diffraction, exploiting the anomalous scattering of a single bromide ion and six of the seven sulfur atoms of IGF-1. The structure reveals a well-defined conformation for much of the C-region, which extends away from the core of IGF-1 and has residues known to be involved in receptor binding prominently displayed in a type II beta-turn. In the crystal, these residues form a dimer interface, but analytical ultracentrifugation experiments demonstrate that at physiological concentrations IGF-1 is monomeric. A single detergent molecule contacts residues known to be important for IGF-1 binding protein (IGFBP) interactions. Biophysical and biochemical data show that the detergent binds to IGF-1 specifically and blocks binding of IGFBP-1 and IGFBP-3.
About this Structure
1IMX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions., Vajdos FF, Ultsch M, Schaffer ML, Deshayes KD, Liu J, Skelton NJ, de Vos AM, Biochemistry. 2001 Sep 18;40(37):11022-9. PMID:11551198 Page seeded by OCA on Fri May 2 20:10:18 2008