X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain

<div><p>Chitinases are enzymes that catalyze the hydrolysis of chitin. Human chitotriosidase (CHIT1) is one of the two active human chitinases, involved in the innate immune response and highly expressed in a variety of diseases. CHIT1 is composed of a catalytic domain linked by a hinge...

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Bibliographic Details
Main Author:	Firas Fadel (2625211) (author)
Other Authors:	Yuguang Zhao (229106) (author), Alexandra Cousido-Siah (777034) (author), Francesc X. Ruiz (777032) (author), André Mitschler (2625214) (author), Alberto Podjarny (777035) (author)
Published:	2016
Subjects:	Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Evolutionary Biology Immunology Developmental Biology Cancer Infectious Diseases Plant Biology Virology Computational Biology Chemical Sciences not elsewhere classified house mite dust allergens CBM 14 family members Full Length Human Chitotriosidase Human chitotriosidase length CHIT 1 CBM 14 domain CHIT 1 ChBD CHIT 1 CBM 14 family crystallization approach chitin binding domain latter domain Acidic Mammalian Chitinase 1.95 Å resolution crystal structure Chitin Binding Domain Chitinases disulfide bridges Trp 465 crystal structures chitin binding chitinase CHIT 1 cysteine residues crystallization strategy CHIT 1 chitin binding domain
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X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain

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