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Figure 2
Mapping residues that are conserved between Nas2 and the human ortholog PSMD9. (a) Alignment of Nas2 PDZ-domain residues with the human ortholog PSMD9. Residues modeled in the crystal structure of Nas2 were used in a BLASTp search against the human protein RefSeq database. The top hit was the human ortholog of Nas2, PSMD9, showing 42% identity and 64% conserved residues (the latter are indicated with +). (b) Graphic structure of Nas2 in green. Based on an alignment between Nas2 and PSMD9, conserved residues were colored orange and identical residues red. The cloning-derived residues are in blue. (c) Surface representation of (b). Note the conservation in the groove of the PDZ domain between α-helix 2 and β-strand 5. In PDZ-domain proteins this region commonly binds peptides/C-termini from their binding partner.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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