Open AccessCocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide
Author(s) -
Liu Weizhi,
Boggon Titus J.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113010762
Subject(s) - integrin , cocrystal , cytoplasm , integrin, beta 6 , resolution (logic) , chemistry , microbiology and biotechnology , biophysics , biology , biochemistry , hydrogen bond , molecule , cell , organic chemistry , artificial intelligence , computer science
Integrin cytoplasmic domain‐associated protein‐1 (ICAP1) is a suppressor of integrin activation and directly binds to the cytoplasmic tail of β1 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 Å resolution [the resolution at which 〈 I /σ( I )〉 = 2.9 was 1.83 Å]. In previous studies, the structure of ICAP1 with integrin β1 was determined to 3.0 Å resolution and that of ICAP1 with the N‐terminal portion of KRIT1 (residues 1–198) was determined to 2.54 Å 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.