MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5. The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5. EMBO J. (0261-4189) 2001 Zesławski W., Beisel HG., Kamionka M., Kalus W., Engh RA., Huber R., Lang K., Holak TA. no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Zesławski W., Beisel HG., Kamionka M., Kalus W., Engh RA., Huber R., Lang K., Holak TA. no EMBO J. (0261-4189) 2001 ibp5_rat Insulin-like growth factor-binding protein 5 Igfbp5 Igfbp-5 protein protein rat Rattus norvegicus (Rat) Rat MVISVVLLLLAACAVPAQGLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYGEQTKIERDSREHEEPTTSEMAEETYSPKVFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRVIPAPEMRQESDQGPCRRHMEASLQEFKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHAFDSSNVE mint IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors 545B4C48F9BB5493 igf1_human Insulin-like growth factor I IGF1 IBP1 Somatomedin-C Mechano growth factor protein protein human Homo sapiens Human MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK DIP protein P05019 original sequence version: 130 DIP protein P05019 original sequence version: 178 DIP protein P05019 original sequence version: 140 DIP protein P05019 original sequence version: 186 DIP protein P05019 original sequence version: 151 The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]. IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation mint E88A8CFBD1CD1873 igf1-igfbp5 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1h59, P05019 is chain A and P24594 is chain B Resolution 2.100 homomint mint