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1boe

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{{STRUCTURE_1boe| PDB=1boe | SCENE= }}
{{STRUCTURE_1boe| PDB=1boe | SCENE= }}
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'''STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR INTERACTIONS'''
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===STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR INTERACTIONS===
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==Overview==
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Binding proteins for insulin-like growth factors (IGFs) IGF-I and IGF-II, known as IGFBPs, control the distribution, function and activity of IGFs in various cell tissues and body fluids. Insulin-like growth factor-binding protein-5 (IGFBP-5) is known to modulate the stimulatory effects of IGFs and is the major IGF-binding protein in bone tissue. We have expressed two N-terminal fragments of IGFBP-5 in Escherichia coli; the first encodes the N-terminal domain of the protein (residues 1-104) and the second, mini-IGFBP-5, comprises residues Ala40 to Ile92. We show that the entire IGFBP-5 protein contains only one high-affinity binding site for IGFs, located in mini-IGFBP-5. The solution structure of mini-IGFBP-5, determined by nuclear magnetic resonance spectroscopy, discloses a rigid, globular structure that consists of a centrally located three-stranded anti-parallel beta-sheet. Its scaffold is stabilized further by two inside packed disulfide bridges. The binding to IGFs, which is in the nanomolar range, involves conserved Leu and Val residues localized in a hydrophobic patch on the surface of the IGFBP-5 protein. Remarkably, the IGF-I receptor binding assays of IGFBP-5 showed that IGFBP-5 inhibits the binding of IGFs to the IGF-I receptor, resulting in reduction of receptor stimulation and autophosphorylation. Compared with the full-length IGFBP-5, the smaller N-terminal fragments were less efficient inhibitors of the IGF-I receptor binding of IGFs.
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(as it appears on PubMed at http://www.pubmed.gov), where 9822601 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9822601}}
==About this Structure==
==About this Structure==
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1BOE is a [[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=1BOE OCA].
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1BOE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOE OCA].
==Reference==
==Reference==
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[[Category: Mini-igfbp-5]]
[[Category: Mini-igfbp-5]]
[[Category: Nmr]]
[[Category: Nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:45:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:27:21 2008''

Revision as of 16:27, 30 June 2008

Image:1boe.png

Template:STRUCTURE 1boe

STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR INTERACTIONS

Template:ABSTRACT PUBMED 9822601

About this Structure

1BOE is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions., Kalus W, Zweckstetter M, Renner C, Sanchez Y, Georgescu J, Grol M, Demuth D, Schumacher R, Dony C, Lang K, Holak TA, EMBO J. 1998 Nov 16;17(22):6558-72. PMID:9822601

Page seeded by OCA on Mon Jun 30 19:27:21 2008

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