1h02: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1H02 is a | 1H02 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]. The following page contains interesting information on the relation of 1H02 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb52_1.html Growth Hormone]]. Structure known Active Site: C15. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H02 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plasma]] | [[Category: plasma]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:34:41 2007'' | ||
Revision as of 14:29, 5 November 2007
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HUMAN INSULIN-LIKE GROWTH FACTOR; SRS DARESBURY 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.
About this StructureAbout this Structure
1H02 is a Single protein structure of sequence from Homo sapiens with C15 as ligand. The following page contains interesting information on the relation of 1H02 with [Growth Hormone]. Structure known Active Site: C15. 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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