1gzr: Difference between revisions
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[[Image:1gzr.gif|left|200px]]<br /><applet load="1gzr" size=" | [[Image:1gzr.gif|left|200px]]<br /><applet load="1gzr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gzr, resolution 2.00Å" /> | caption="1gzr, resolution 2.00Å" /> | ||
'''HUMAN INSULIN-LIKE GROWTH FACTOR; ESRF DATA'''<br /> | '''HUMAN INSULIN-LIKE GROWTH FACTOR; ESRF DATA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1GZR 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 C15 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=C15:C15 Binding Site For Chain B'>C15</scene>. Full crystallographic information is available from [http:// | 1GZR 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=C15:'>C15</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=C15:C15+Binding+Site+For+Chain+B'>C15</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plasma]] | [[Category: plasma]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:44:28 2008'' | ||
Revision as of 10:44, 3 February 2008
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HUMAN INSULIN-LIKE GROWTH FACTOR; ESRF DATA
OverviewOverview
Human insulin-like growth factors I and II (hIGF-I, hIGF-II) are potent, stimulators of cell and growth processes. They display high sequence, similarity to both the A and B chains of insulin but contain an additional, connecting C-domain, which reflects their secretion without specific, packaging or precursor conversion. IGFs also have an extension at the, C-terminus known as the D-domain. This paper describes four homologous, hIGF-1 structures, obtained from crystals grown in the presence of the, detergent SB12, which reveal additional detail in the C- and D-domains., Two different detergent binding modes observed in the crystals may reflect, different hIGF-I biological properties such as the interaction with IGF, binding proteins and self-aggregation. While the helical core of hIGF-I is, very similar to that in insulin, there are distinct differences in the, region of hIGF-I corresponding to the insulin B chain C-terminus, residues, B25-B30. In hIGF-I, these residues (24-29) and the following C-domain form, an extensive loop protruding 20 A from the core, which results in a, substantially different conformation for the receptor binding epitope in, hIGF-I compared to insulin. One notable feature of the structures, presented here is demonstration of peptide-bond cleavage between Ser35 and, Arg36 resulting in an apparent gap between residues 35 and 39. The, equivalent region of proinsulin is involved in hormone processing, demanding a reassessment of the structural integrity of hIGF-I in relation, to its biological function.
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
1GZR is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structural origins of the functional divergence of human insulin-like growth factor-I and insulin., Brzozowski AM, Dodson EJ, Dodson GG, Murshudov GN, Verma C, Turkenburg JP, de Bree FM, Dauter Z, Biochemistry. 2002 Jul 30;41(30):9389-97. PMID:12135360
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