Neprilysin 2 is a recently identified glycoprotein displaying the highest degree of sequence identity with neprilysin (EC 22.214.171.124), the prototypical member of the M13 family of zinc-dependent metalloproteases. Whereas neprilysin has been shown to be involved in the inactivation of endogenous messenger peptides, like enkephalins and tachykinins, the true physiological functions of neprilysin 2 remain unknown.
Unite de Neurobiologie et Pharmacologie Moleculaire (U573) de l'INSERM. Centre Paul Broca, 2ter rue d'Alesia, 75014 Paris, France.
Publication date: October 1, 2004
More about this publication?
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.