Structural highlights
FunctionITBP1_HUMAN Regulates integrin signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. May play a role in the recruitment of ITGB1 to focal contacts during integrin-dependent cell adhesion.[REFERENCE:8] Publication Abstract from PubMedIntegrin cytoplasmic domain-associated protein-1 (ICAP1) is a suppressor of integrin activation and directly binds to the cytoplasmic tail of beta1 integrins; its binding suppresses integrin activation by competition with talin. Krev/Rap1 interaction trapped-1 (KRIT1) releases ICAP1 suppression of integrin activation by sequestering ICAP1 away from integrin cytoplasmic tails. Here, the cocrystal structure of the PTB domain of ICAP1 in complex with a 29-amino-acid fragment (residues 170-198) of KRIT1 is presented to 1.7 A resolution [the resolution at which I/sigma(I) = 2.9 was 1.83 A]. In previous studies, the structure of ICAP1 with integrin beta1 was determined to 3.0 A resolution and that of ICAP1 with the N-terminal portion of KRIT1 (residues 1-198) was determined to 2.54 A resolution; therefore, this study provides the highest resolution structure yet of ICAP1 and allows further detailed analysis of the interaction of ICAP1 with its minimal binding region in KRIT1. Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide.,Liu W, Boggon TJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):494-8. doi:, 10.1107/S1744309113010762. Epub 2013 Apr 27. PMID:23695561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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