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Article

The X-ray crystal structure of full-length human plasminogen.

Cell reports - 29 Mar 2012

Law Ruby H P, Caradoc-Davies Tom, Cowieson Nathan, Horvath Anita J, Quek Adam J, Encarnacao Joanna Amarante, Steer David, Cowan Angus, Zhang Qingwei, Lu Bernadine G C, Pike Robert N, Smith A Ian, Coughlin Paul B, Whisstock James C

Abstract excerpt

Plasminogen is the proenzyme precursor of the primary fibrinolytic protease plasmin. Circulating plasminogen, which comprises a Pan-apple (PAp) domain, five kringle domains (KR1-5), and a serine protease (SP) domain, adopts a closed, activation-resistant conformation. The kringle domains mediate interactions with fibrin clots and cell-surface receptors. These interactions trigger plasminogen to adopt an open form...

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Share to Crystallography, X-Ray
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22832192
DOI: 10.1016/j.celrep.2012.02.012

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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