1NPM

NEUROPSIN, A SERINE PROTEASE EXPRESSED IN THE LIMBIC SYSTEM OF MOUSE BRAIN

Summary for 1NPM

• Entry DOI: 10.2210/pdb1npm/pdb
• Descriptor: NEUROPSIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: serine proteinase, glycoprotein
• Biological source: Mus musculus (house mouse)
• Cellular location: Secreted: Q61955
• Total number of polymer chains: 2
• Total formula weight: 49850.51

Authors

Kishi, T.,Kato, M.,Shimizu, T.,Kato, K.,Matsumoto, K.,Yoshida, S.,Shiosaka, S.,Hakoshima, T. (deposition date: 1998-01-07, release date: 1999-03-23, Last modification date: 2024-10-30)

Primary citation

Kishi, T.,Kato, M.,Shimizu, T.,Kato, K.,Matsumoto, K.,Yoshida, S.,Shiosaka, S.,Hakoshima, T.
Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.
J.Biol.Chem., 274:4220-4224, 1999

PubMed Abstract: Neuropsin is a novel serine protease, the expression of which is highly localized in the limbic areas of the mouse brain and which is suggested to be involved in kindling epileptogenesis and hippocampal plasticity. The 2.1-A resolution crystal structure of neuropsin provides the first three-dimensional view of one of the serine proteases highly expressed in the nervous system, and reveals a serine protease fold that exhibits chimeric features between trypsin and nerve growth factor-gamma (NGFgamma), a member of the kallikrein family. Neuropsin possesses an N-glycosylated "kallikrein loop" but forms six disulfide bonds corresponding to those of trypsin. The ordered kallikrein loop projects proline toward the active site to restrict smaller residues or proline at the P2 position of substrates. Loop F, which participates in forming the S3/S4 sites, is similar to trypsin rather than NGFgamma. The unique conformations of loops G and H form an S1 pocket specific for both arginine and lysine. These characteristic loop structures forming the substrate-binding site suggest the novel substrate specificity of neuropsin and give a clue to the design of its specific inhibitors.

PubMed: 9933620
DOI: 10.1074/jbc.274.7.4220

Experimental method

X-RAY DIFFRACTION (2.1 Å)