4dd8
ADAM-8 metalloproteinase domain with bound batimastatADAM-8 metalloproteinase domain with bound batimastat
Structural highlights
FunctionADAM8_HUMAN Possible involvement in extravasation of leukocytes. Publication Abstract from PubMedThe role of ADAM-8 in cancer and inflammatory diseases such as allergy, arthritis and asthma makes it an attractive target for drug development. Therefore, the catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme-inhibitor complex was refined to 2.1 A resolution. ADAM-8 has an overall fold similar to those of other ADAM members, including a central five-stranded beta-sheet and a catalytic Zn(2+) ion. However, unique differences within the S1' binding loop of ADAM-8 are observed which might be exploited to confer specificity and selectivity to ADAM-8 competitive inhibitors for the treatment of diseases involving this enzyme. Structure of human ADAM-8 catalytic domain complexed with batimastat.,Hall T, Shieh HS, Day JE, Caspers N, Chrencik JE, Williams JM, Pegg LE, Pauley AM, Moon AF, Krahn JM, Fischer DH, Kiefer JR, Tomasselli AG, Zack MD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):616-21., Epub 2012 May 22. PMID:22684055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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