» Articles » PMID: 23695561

Cocrystal Structure of the ICAP1 PTB Domain in Complex with a KRIT1 Peptide

Overview
Date 2013 May 23
PMID 23695561
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

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.

Citing Articles

KRIT1 in vascular biology and beyond.

Glading A Biosci Rep. 2024; 44(7).

PMID: 38980708 PMC: 11263069. DOI: 10.1042/BSR20231675.


Serine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation.

Su V, Simon B, Draheim K, Calderwood D J Biol Chem. 2020; 295(10):3269-3284.

PMID: 32005669 PMC: 7062153. DOI: 10.1074/jbc.RA119.009794.


Recent advances in cerebral cavernous malformation research.

Padarti A, Zhang J Vessel Plus. 2019; 2.

PMID: 31360916 PMC: 6663315. DOI: 10.20517/2574-1209.2018.34.


Nuclear Localization of Integrin Cytoplasmic Domain-associated Protein-1 (ICAP1) Influences β1 Integrin Activation and Recruits Krev/Interaction Trapped-1 (KRIT1) to the Nucleus.

Draheim K, Huet-Calderwood C, Simon B, Calderwood D J Biol Chem. 2016; 292(5):1884-1898.

PMID: 28003363 PMC: 5290960. DOI: 10.1074/jbc.M116.762393.


Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface.

Zhang R, Li X, Boggon T J Struct Biol. 2015; 192(3):449-456.

PMID: 26458359 PMC: 4651721. DOI: 10.1016/j.jsb.2015.10.006.


References
1.
McCoy A, Grosse-Kunstleve R, Storoni L, Read R . Likelihood-enhanced fast translation functions. Acta Crystallogr D Biol Crystallogr. 2005; 61(Pt 4):458-64. DOI: 10.1107/S0907444905001617. View

2.
Murshudov G, Skubak P, Lebedev A, Pannu N, Steiner R, Nicholls R . REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr. 2011; 67(Pt 4):355-67. PMC: 3069751. DOI: 10.1107/S0907444911001314. View

3.
Cavalcanti D, Kalani M, Martirosyan N, Eales J, Spetzler R, Preul M . Cerebral cavernous malformations: from genes to proteins to disease. J Neurosurg. 2011; 116(1):122-32. DOI: 10.3171/2011.8.JNS101241. View

4.
Li J, Mao X, Dong L, Liu F, Tong L . Crystal structures of the BAR-PH and PTB domains of human APPL1. Structure. 2007; 15(5):525-33. DOI: 10.1016/j.str.2007.03.011. View

5.
McNicholas S, Potterton E, Wilson K, Noble M . Presenting your structures: the CCP4mg molecular-graphics software. Acta Crystallogr D Biol Crystallogr. 2011; 67(Pt 4):386-94. PMC: 3069754. DOI: 10.1107/S0907444911007281. View