1b9g: Difference between revisions
New page: left|200px<br /> <applet load="1b9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b9g" /> '''INSULIN-LIKE-GROWTH-FACTOR-1'''<br /> ==Ov... |
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[[Image:1b9g.gif|left|200px]]<br /> | [[Image:1b9g.gif|left|200px]]<br /><applet load="1b9g" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''INSULIN-LIKE-GROWTH-FACTOR-1'''<br /> | '''INSULIN-LIKE-GROWTH-FACTOR-1'''<br /> | ||
==Overview== | ==Overview== | ||
Mini insulin-like growth factor 1, an inactive insulin-like growth factor | Mini insulin-like growth factor 1, an inactive insulin-like growth factor 1 mutant lacking the C region, was studied by 2D NMR spectroscopy. Resonances were assigned for almost all protons of the 57 amino acid residues. The 3D structure of the protein was determined by distance geometry methods. Three helical segments; Ala 8-Cys 18, Gly 42-Phe 49, and Leu 54-Cys 61, were identified, corresponding to those present in wild-type insulin-like growth factor 1 and in single-chain insulin. Their relative orientation, however, was found to be changed. This change is connected with a displacement of the Phe 23-Tyr 24-Phe 25-Asn 26 beta-strand-like segment, i.e., of aromatic side chains known to be important for receptor binding. Thus, deletion of the C region of IGF-1 results in a substantial tertiary structural rearrangement that accounts for the loss of receptor affinity. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1B9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1B9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9G OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Grotzinger, J.]] | [[Category: Grotzinger, J.]] | ||
[[Category: Pitts, J.]] | [[Category: Pitts, J.]] | ||
[[Category: Wolf, E | [[Category: Wolf, E De.]] | ||
[[Category: Wollmer, A.]] | [[Category: Wollmer, A.]] | ||
[[Category: growth factor igf-1]] | [[Category: growth factor igf-1]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:54 2008'' | ||
Revision as of 12:52, 21 February 2008
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INSULIN-LIKE-GROWTH-FACTOR-1
OverviewOverview
Mini insulin-like growth factor 1, an inactive insulin-like growth factor 1 mutant lacking the C region, was studied by 2D NMR spectroscopy. Resonances were assigned for almost all protons of the 57 amino acid residues. The 3D structure of the protein was determined by distance geometry methods. Three helical segments; Ala 8-Cys 18, Gly 42-Phe 49, and Leu 54-Cys 61, were identified, corresponding to those present in wild-type insulin-like growth factor 1 and in single-chain insulin. Their relative orientation, however, was found to be changed. This change is connected with a displacement of the Phe 23-Tyr 24-Phe 25-Asn 26 beta-strand-like segment, i.e., of aromatic side chains known to be important for receptor binding. Thus, deletion of the C region of IGF-1 results in a substantial tertiary structural rearrangement that accounts for the loss of receptor affinity.
DiseaseDisease
Known disease associated with this structure: Growth retardation with deafness and mental retardation due to IGF1 deficiency OMIM:[147440]
About this StructureAbout this Structure
1B9G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of a mini IGF-1., De Wolf E, Gill R, Geddes S, Pitts J, Wollmer A, Grotzinger J, Protein Sci. 1996 Nov;5(11):2193-202. PMID:8931138
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