9PX9

ATTR V122I cardiac amyloid fibrils

Summary for 9PX9

• Entry DOI: 10.2210/pdb9px9/pdb
• EMDB information: 71962
• Descriptor: Transthyretin (1 entity in total)
• Functional Keywords: transthyretin, amyloidosis, protein fibril
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 6
• Total formula weight: 95514.07

Authors

Schaefer, J.H.,Lander, G.C. (deposition date: 2025-08-05, release date: 2026-05-13)

Primary citation

Donnelly, J.P.,Schafer, J.H.,Yoon, L.,Massey, L.A.,Ash, C.,Gao, Z.,Nugroho, K.,Jager, M.,Pang, Z.,O'Neill, R.T.,Maurer, M.S.,Powers, E.T.,Lander, G.C.,Ye, L.,Kelly, J.W.
Three-Dimensional Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary Occlusion.
J Am Heart Assoc, :e042248-e042248, 2026

PubMed Abstract: Transthyretin amyloidosis (ATTR) is a degenerative disease affecting the heart and other organs. Transthyretin (TTR) aggregation is a driver of ATTR pathology, but the mechanism is poorly understood. We used proteomics and tissue clearing technology on wild-type (WT) human cardiac (WT/WT) and V122I human cardiac (V122I/WT) tissue to better understand TTR cardiomyopathy.

PubMed: 42089154
DOI: 10.1161/JAHA.125.042248

Experimental method

ELECTRON MICROSCOPY (3 Å)