Table 2 Characteristics of the APN structures.

From: Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection

Structure

pAPN

hAPN

pAPN-RBD

Conformation

closed

intermediate

open

Intermonomer distance

95 Å

116 Å

131 Å

Interdomain surfaces (Å2)

 DI-DII

1732

1729

1686

 DII-DIII

1341

1329

1243

 DIII-DIV

1161

1121

1016

 DIV-DI

163

8

—

 DIV-DII

1754

1126

754

 DIV-DIV

939

928

981

Interdomain angles

0

6°

15°

  1. Intermonomer distances in the APN dimers were determined between the N-terminal residues of first β-strands. Interdomain buried surfaces in the crystal structures were computed with the PISA server (http://www.ebi.ac.uk/msd-srv/prot_int/cgi-bin/piserver). The domain IV buried surface in each monomer at the dimer interface is shown as DIV-DIV. Interdomain angles of the open and intermediate structures were determined relative to the closed pAPN after structure superposition based on domain IV. Angles were computed based on the zinc ions at domain II and the hinge residue at the domain IV N terminus with the COOT program41. The pAPNeh structure has very similar conformation to the native pAPN.
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