1h8l

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spinqualitylabelsall models 1h8l, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DUCK CARBOXYPEPTIDASE D DOMAIN II IN COMPLEX WITH GEMSA

Overview

The three-dimensional crystal structure of duck carboxypeptidase D domain, II has been solved in a complex with the peptidomimetic inhibitor, guanidinoethylmercaptosuccinic acid, occupying the specificity pocket., This structure allows a clear definition of the substrate binding sites, and the substrate funnel-like access. The structure of domain II is the, only one available from the regulatory carboxypeptidase family and can be, used as a general template for its members. Here, it has been used to, model the structures of domains I and III from the former protein and of, human carboxypeptidase E. The models obtained show that the overall, topology is similar in all cases, the main differences being local and, because of insertions in non-regular loops. In both carboxypeptidase D, domain I and carboxypeptidase E slightly different shapes of the access to, the active site are predicted, implying some kind of structural selection, of protein or peptide substrates. Furthermore, emplacement of the, inhibitor structure in the active site of the constructed models showed, that the inhibitor fits very well in all of them and that the relevant, interactions observed with domain II are conserved in domain I and, carboxypeptidase E but not in the non-active domain III because of the, absence of catalytically indispensable residues in the latter protein., However, in domain III some of the residues potentially involved in, substrate binding are well preserved, together with others of unknown, roles, which also are highly conserved among all carboxypeptidases. These, observations, taken together with others, suggest that domain III might, play a role in the binding and presentation of proteins or peptide, substrates, such as the pre-S domain of the large envelope protein of duck, hepatitis B virus.

About this Structure

1H8L is a Single protein structure of sequence from Anas specularioides with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases., Aloy P, Companys V, Vendrell J, Aviles FX, Fricker LD, Coll M, Gomis-Ruth FX, J Biol Chem. 2001 May 11;276(19):16177-84. Epub 2001 Feb 14. PMID:11278909

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