First-pass extracted concept

alphaIIb integrin cytoplasmic domain

Candidate: toolkit item1 source documents3 linked claims

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Aliases

alphaIIb cytoplasmic domain

Evidence Snippets

the alphaIIb cytoplasmic domain of platelet integrin alphaIIbbeta3

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2006Journal of Biological ChemistryDOI PubMed

1 evidence snippet 3 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1binding site mappingsupports2006Source 1locatorDOI PubMed

The alphaIIb-binding site on CIB1 is a hydrophobic channel spanning the entire C domain and part of the N domain.

Quoted textsource-backed

chemical shift perturbation mapping has identified the alphaIIb-binding site as a hydrophobic channel spanning the entire C domain and part of the N domain

Claim 2interaction mechanismsupports2006Source 1locatorDOI PubMed

CIB1 specifically interacts with the alphaIIb integrin cytoplasmic domain.

Quoted textsource-backed

CIB1 regulates platelet aggregation in hemostasis through a specific interaction with the alphaIIb cytoplasmic domain of platelet integrin alphaIIbbeta3.

Claim 3interaction mechanismsupports2006Source 1locatorDOI PubMed

The extreme C-terminal end of CIB1 weakly interacts with the hydrophobic channel in the absence of a biological target and is displaced by the alphaIIb cytoplasmic domain, suggesting a mechanism that increases binding specificity.

Quoted textsource-backed

Data obtained with a truncated version of CIB1 suggest that the extreme C-terminal end of the protein weakly interacts with this channel in the absence of a biological target, but it is displaced by the alphaIIb cytoplasmic domain, suggesting a novel mechanism to increase binding specificity.