A Noncleavable Retro-Binding Peptide That Spans the Substrate Binding Cleft of Serine Proteases. Atomic Structure of Nazumamide A: Human Thrombin

Autor:	Vicki L. Nienaber, Eugene C. Amparo
Rok vydání:	1996
Předmět:	Proteases Natural product Stereochemistry Substrate (chemistry) General Chemistry Crystal structure Binding peptide Biochemistry Catalysis Serine chemistry.chemical_compound Crystallography Colloid and Surface Chemistry chemistry Human Thrombin MASP1
Zdroj:	Journal of the American Chemical Society. 118:6807-6810
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja960045t
Popis:	The 2.0 A resolution crystal structure of the retro-binding natural product nazumamide A (NAZA) complexed with human thrombin is presented. The crystal structure shows that the retro-binding nazumamide A is noncleavable and extends into the prime end of the substrate binding cleft. The data suggest ideas for SAR and combinatorial modification of nazumamide A to create a second generation of nazumamide-like compounds which are potent and specific for human thrombin. This crystal structure indicates that fresh ideas for the generation of novel and specific inhibitors may arise from examining weak binding compounds. Additionally, the crystal structure demonstrates the utility of crystallographic analysis of natural product:protein complexes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e43aa7ffee2a96d6d2a13ee7e11c0500 https://doi.org/10.1021/ja960045t Zobrazit plný text záznamu