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Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide.

ABSTRACT: Integrin cytoplasmic domain-associated protein-1 (ICAP1) is a suppressor of integrin activation and directly binds to the cytoplasmic tail of ?1 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/?(I)? = 2.9 was 1.83?Å]. In previous studies, the structure of ICAP1 with integrin ?1 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.

SUBMITTER: Liu W

PROVIDER: S-EPMC3660885 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide.

Liu Weizhi W Boggon Titus J TJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20130427 Pt 5

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 KRIT ...[more]

PMID: 23695561

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