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Glaeser RM. Human tripeptidyl peptidase II: a gentle giant. Structure. 2012;20(4):565-6doi: 10.1016/j.str.2012.03.002.
Glaeser, R. M. (2012). Human tripeptidyl peptidase II: a gentle giant. Structure (London, England : 1993), 20(4), 565-6. https://doi.org/10.1016/j.str.2012.03.002
Glaeser, Robert M. "Human tripeptidyl peptidase II: a gentle giant." Structure (London, England : 1993) vol. 20,4 (2012): 565-6. doi: https://doi.org/10.1016/j.str.2012.03.002
Glaeser RM. Human tripeptidyl peptidase II: a gentle giant. Structure. 2012 Apr 04;20(4):565-6. doi: 10.1016/j.str.2012.03.002. Epub 2012 Apr 03. PMID: 22483101.
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Structure. 2012 Apr 04;20(4):565-6. doi: 10.1016/j.str.2012.03.002. Epub 2012 Apr 03.

Human tripeptidyl peptidase II: a gentle giant.

Structure (London, England : 1993)

Robert M Glaeser

Affiliations

  1. Donner Laboratory, Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA. [email protected]

PMID: 22483101 DOI: 10.1016/j.str.2012.03.002

Abstract

Molecular structures can serve to either validate or rule out existing hypotheses, and they can also spawn new, deeper proposals about biochemical mechanism. In this issue of Structure, Schönegge et al. use single-particle cryo-electron microscopy and flexible docking to examine the function of human tripeptidyl peptidase II, including the role of conformational changes in enzyme activation.

Copyright © 2012 Elsevier Ltd. All rights reserved.

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