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Table 1 Interacting residues of NAP–histone complexes

From: Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones

 

Histone-binding residues of NAP

Histone H2A residues that bind to NAP

Histone H2B residues that bind to NAP

  

Xenopus laevis H2A–H2B

ScNAP1

P197, I198, C200, D201, D205, P308, E310, E328, E332, E336, A339

T16, R17, R20, P26, R29, R35, K75, R77, R81, Q105

I36, Y37

  

C. elegans H2B 1–H2A fusion protein

CeNAP1

Q7, M9, L12, T14, D17, Q20, D125, A128, E129, I131, E132, S294, D295, D296

S131, R132, G143, R144, R147, R150, K151

S33, S35, V36, Y37, Y39, R40, S53, M56, S57

  

A.thaliana H2A–H2B

AtNRP1

E32, E36, D39, D40, K43, I44, E46

R29, R32, F33, A36

V58, E59, T60, K62, I63, Y64

  1. Histone-binding residues of NAPs and NAP-binding residues of histone H2A–H2B based on the three three-dimensional structures of NAP–histone complex—S. cerevisiae (ScNAP1; PDB ID: 5G2E), C. elegans (CeNAP1; PDB ID: 6K00) and A. thaliana (AtNRP1; PDB ID: 7C7X). Italicized residues belong to fusion protein H2B 1–H2A