3FXY

Acidic Mammalian Chinase, Catalytic Domain

Summary for 3FXY

• Entry DOI: 10.2210/pdb3fxy/pdb
• Related: 3FY1
• Descriptor: Acidic mammalian chitinase (2 entities in total)
• Functional Keywords: chitinase, asthma, chitin degradation, alternative splicing, carbohydrate metabolism, chitin-binding, cytoplasm, glycosidase, hydrolase, polymorphism, polysaccharide degradation, secreted
• Biological source: Homo sapiens (human)
• Cellular location: Secreted. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm: Q9BZP6
• Total number of polymer chains: 4
• Total formula weight: 176813.48

Authors

Olland, A.M. (deposition date: 2009-01-21, release date: 2009-03-10, Last modification date: 2024-10-16)

Primary citation

Olland, A.M.,Strand, J.,Presman, E.,Czerwinski, R.,Joseph-McCarthy, D.,Krykbaev, R.,Schlingmann, G.,Chopra, R.,Lin, L.,Fleming, M.,Kriz, R.,Stahl, M.,Somers, W.,Fitz, L.,Mosyak, L.
Triad of polar residues implicated in pH specificity of acidic mammalian chitinase.
Protein Sci., 18:569-578, 2009

PubMed Abstract: Acidic mammalian chitinase (AMCase) is a mammalian chitinase that has been implicated in allergic asthma. One of only two active mammalian chinases, AMCase, is distinguished from other chitinases by several unique features. Here, we present the novel structure of the AMCase catalytic domain, both in the apo form and in complex with the inhibitor methylallosamidin, determined to high resolution by X-ray crystallography. These results provide a structural basis for understanding some of the unique characteristics of this enzyme, including the low pH optimum and the preference for the beta-anomer of the substrate. A triad of polar residues in the second-shell is found to modulate the highly conserved chitinase active site. As a novel target for asthma therapy, structural details of AMCase activity will help guide the future design of specific and potent AMCase inhibitors.

PubMed: 19241384
DOI: 10.1002/pro.63

Experimental method

X-RAY DIFFRACTION (2 Å)