2005
DOI: 10.1016/j.str.2004.11.009
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Abstract: Insulin-like growth factor binding proteins (IGFBPs) control the extracellular distribution, function, and activity of IGFs. Here, we report an X-ray structure of the binary complex of IGF-I and the N-terminal domain of IGFBP-4 (NBP-4, residues 3-82) and a model of the ternary complex of IGF-I, NBP-4, and the C-terminal domain (CBP-4, residues 151-232) derived from diffraction data with weak definition of the C-terminal domain. These structures show how the IGFBPs regulate IGF signaling. Key features of the st… Show more

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Cited by 69 publications
(84 citation statements)
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“…We divide this CBP4 interface into three parts based on its interacting partners: the part that makes contacts with IGF1 only, the segment that interacts with both NBP4 and IGF1, and the stretch of residues Glu-168(C)-Glu-173(C) of CBP4 which interacts with the so-called ''thumb'' region of NBP4. The thumb region consists of a short stretch of the very first N-terminal residues of IGFBPs that precede the first N-terminal cysteine (amino acids 1-5 in IGFBP4) (10). It is worth noting that both CBP4 and NBP4 occupy one side, a dome part, of a pear-like IGF1 structure (Figs.…”
Section: Resultsmentioning
confidence: 99%
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“…We divide this CBP4 interface into three parts based on its interacting partners: the part that makes contacts with IGF1 only, the segment that interacts with both NBP4 and IGF1, and the stretch of residues Glu-168(C)-Glu-173(C) of CBP4 which interacts with the so-called ''thumb'' region of NBP4. The thumb region consists of a short stretch of the very first N-terminal residues of IGFBPs that precede the first N-terminal cysteine (amino acids 1-5 in IGFBP4) (10). It is worth noting that both CBP4 and NBP4 occupy one side, a dome part, of a pear-like IGF1 structure (Figs.…”
Section: Resultsmentioning
confidence: 99%
“…NBP4 (residues 1-92) includes now the two first N-terminal thumb residues not present in our previously used NBP4 (residues 3-82) construct (10). Compared with the structure of NBP4(3-82)͞IGF1 (10), to the NBP4(3-82)͞IGF1 part of the NBP4(3-82)͞IGF1͞CBP4 (residues 151-232) and the NBP4(1-82)͞IGF1 of the NBP4(1-92)͞IGF1͞CBP1 (residues 141-234), the four complexes reveal virtually no changes in positions of the backbone and most of the side-chain atoms of both NBP4 and IGF; heavy atom rmsds are 0.75, 0.71, and 0.96 Å respectively. The first two thumb residues are, however, defined only in the binary NBP4(1-92)͞IGF1 complex (Fig.…”
Section: The Nbp4(1-92)͞igf1 Complex and The Ternary Complex Of Cbp1mentioning
confidence: 99%
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“…In addition, IGFBPs 1-5 share a cysteine-rich motif, GCGCCXXC (where X is any amino acid), within the N-terminal domain (6,8,12). Limited insights into the three-dimensional organization of IGFBPs have come from results of high-resolution x-ray crystallographic analyses of the isolated N-terminal domain of IGFBP-4 and the C-terminal segments of IGFBP-1 and IGFBP-4 (13,14). One consistent observation from these data is that IGFBPs lack inter-domain disulfide bonds (12)(13)(14)(15).…”
mentioning
confidence: 99%
“…Limited insights into the three-dimensional organization of IGFBPs have come from results of high-resolution x-ray crystallographic analyses of the isolated N-terminal domain of IGFBP-4 and the C-terminal segments of IGFBP-1 and IGFBP-4 (13,14). One consistent observation from these data is that IGFBPs lack inter-domain disulfide bonds (12)(13)(14)(15). However, as the structure of a fulllength IGFBP has not been solved, possibly because of the dis-ordered nature of the linker segment, this conclusion remains provisional.…”
mentioning
confidence: 99%