From 3d33883a413e62ed6e29aa0cf338ae196f6308bf Mon Sep 17 00:00:00 2001
From: hvaysset <hugo.vaysset@cri-paris.org>
Date: Mon, 18 Dec 2023 20:50:47 +0100
Subject: [PATCH] Fixed ref to image

---
 content/2.general-concepts/6.defensive-domains.md | 2 +-
 1 file changed, 1 insertion(+), 1 deletion(-)

diff --git a/content/2.general-concepts/6.defensive-domains.md b/content/2.general-concepts/6.defensive-domains.md
index c2ca79d7..881cec27 100644
--- a/content/2.general-concepts/6.defensive-domains.md
+++ b/content/2.general-concepts/6.defensive-domains.md
@@ -9,7 +9,7 @@ contributors:
 # What are protein domains ?
 Proteins can typically be decomposed into a set of structural or functional units called "domains" where each individual domain has a specific biological function (e.g. catalyzing a chemical reaction or binding to another protein). The combination of one or several protein domains within a protein determines its biological function. 
 
-![illustration_thsa](/defensive_domain/ThsA.png){max-width=500px}
+![illustration_thsa](/public/defensive_domain/ThsA.png){max-width=500px}
 
 To examplify this idea, the figure is a depiction of the ThsA protein involved in the [Thoeris](/content/3.defense-systems/thoeris.md) defense system in *Bacillus cereus*. The protein is composed of two domains : a SIR2-like domain (blue) and a SLOG domain (green). The SLOG domain of ThsA is able to bind to cyclic Adenosine Diphosphate Ribose (cADPR), a signalling molecule produced by ThsB upon phage infection. Binding of cADPR activates the Nicotinamide Adenine Dinucleotide (NAD) depletion activity of the SIR2-like domain which causes abortive infection. This shows how the presence of two domains in this protein allows it to be activated by the sensor component of the system (ThsB) and to trigger the immune response mechanism :ref{doi=10.1038/s41586-021-04098-7}.
 
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