1imx
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(New page: 200px<br /> <applet load="1imx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imx, resolution 1.82Å" /> '''1.8 Angstrom crysta...) |
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| - | [[Image:1imx.gif|left|200px]]<br /> | + | [[Image:1imx.gif|left|200px]]<br /><applet load="1imx" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1imx, resolution 1.82Å" /> | caption="1imx, resolution 1.82Å" /> | ||
'''1.8 Angstrom crystal structure of IGF-1'''<br /> | '''1.8 Angstrom crystal structure of IGF-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Despite efforts spanning considerably more than a decade, a | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IMX 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 BR and CPQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IMX 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=BR:'>BR</scene> and <scene name='pdbligand=CPQ:'>CPQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Deshayes, K | + | [[Category: Deshayes, K D.]] |
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
| - | [[Category: Schaffer, M | + | [[Category: Schaffer, M L.]] |
| - | [[Category: Skelton, N | + | [[Category: Skelton, N J.]] |
[[Category: Ultsch, M.]] | [[Category: Ultsch, M.]] | ||
| - | [[Category: Vajdos, F | + | [[Category: Vajdos, F F.]] |
| - | [[Category: Vos, A | + | [[Category: Vos, A M.de.]] |
[[Category: BR]] | [[Category: BR]] | ||
[[Category: CPQ]] | [[Category: CPQ]] | ||
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[[Category: insulin/relaxin]] | [[Category: insulin/relaxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:34 2008'' |
Revision as of 11:13, 21 February 2008
|
1.8 Angstrom crystal structure of IGF-1
Contents |
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.
Disease
Known disease associated with this structure: Growth retardation with deafness and mental retardation due to IGF1 deficiency OMIM:[147440]
About this Structure
1IMX is a Single protein structure of sequence from Homo sapiens with and as ligands. 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 Thu Feb 21 13:13:34 2008