Motion in Heparin Cofactor II [hc2]

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Classification [S-a-2]


Similar to antithrombin (AT). Movement in subunit of HCII dimer includes the expulsion of the reactive center loop, closure of beta -sheet A, and the consequent release of the acidic tail. Multistep allosteric mechanism implied by conformational changes.

Trevor P Baglin, Robin W Carrell, Frank C Church, Charles T Esmon, James A Huntington (2002). Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci U S A, 99:11079-84 [Medline info for 12169660]

GO terms associated with structures
Molecular functionthrombin activity, chymotrypsin activity, trypsin activity, calcium ion binding, serine-type endopeptidase inhibitor activity
Cellular componentextracellular region
Biological processproteolysis and peptidolysis, blood coagulation


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Best representative
Morph Morph name Structure #1 Structure #2 Residues
S195A thrombin-complexed heparin cofacto 1jmj [ A ] 1jmo [ A ] 478

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Email: Mark.Gerstein _at_