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Article

A region in domain II of the urokinase receptor required for urokinase binding.

The Journal of biological chemistry - 15 Sept 2000

Bdeir K, Kuo A, Mazar A, Sachais B S, Xiao W, Gawlak S, Harris S, Higazi A A, Cines D B

Abstract excerpt

The urokinase receptor is composed of three homologous domains based on disulfide spacing. The contribution of each domain to the binding and activation of single chain urokinase (scuPA) remains poorly understood. In the present paper we examined the role of domain II (DII) in these processes. Repositioning DII to the amino or carboxyl terminus of the molecule abolished binding of scuPA as did deleting the domain...

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Identifiers

PMID: 10864923
DOI: 10.1074/jbc.M001595200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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