Mutational dynamics of murine angiogenin duplicates

Table 2 Identification of functionally important residues using co-evolutionary analyses

Pairs	Coevolution Group	Conserved Sites (4Å close)	Active Site	Binding Site	Putative Binding Site	Nuclear Implications
D41-K82	G9	H84, Q93, R95	K40, D41, I42, C92	T80, C81, K82, R121	-	-
K73-N102	G10, G13	S74, S75, N102	-	R101	I56, N63, R70, I71, S72, K73, R101
K82-Q93	G15	D23, H84, Q93, R95, A96	K40, D41, C92	C81, K82	-	C26, E27
K82-T97	G15	D23, H84, R95, A96, T97, R122	-	T44, T79, C81, K82, F120	-	C26
H84-Q93	G12, G16	D23, H84, G86, P91, Q93, R95, A96	C39, K40, D41, S87, C92	C81, K82	-	E27, C39
H84-T97	G12, G16	D23, H84, R95, A96, T97	-	C81, K82	-	-
W89-Q93	G16	T36, G86, W89, P90, P91, Q93	C39, K40, S87, C92	-	-	-
T97-A98	G12, G15	R21, D22, H47, Q77, R95, A96, T97, A98, G99, F100	-	V78, T79, T80, C81	V78	C26
D41-K82	G9	H84, Q93, R95	K40, D41, I42, C92	T80, C81, K82, R121	-	-
K73-N102	G10, G13	S74, S75, N102	-	R101	I56, N63, R70, I71, S72, K73, R101
K82-Q93	G15	D23, H84, Q93, R95, A96	K40, D41, C92	C81, K82	-	C26, E27
K82-T97	G15	D23, H84, R95, A96, T97, R122	-	T44, T79, C81, K82, F120	-	C26
H84-Q93	G12, G16	D23, H84, G86, P91, Q93, R95, A96	C39, K40, D41, S87, C92	C81, K82	-	E27, C39
H84-T97	G12, G16	D23, H84, R95, A96, T97	-	C81, K82	-	-
W89-Q93	G16	T36, G86, W89, P90, P91, Q93	C39, K40, S87, C92	-	-	-
T97-A98	G12, G15	R21, D22, H47, Q77, R95, A96, T97, A98, G99, F100	-	V78, T79, T80, C81	V78	C26

We identify highly conserved amino acid sites (labeled in one-letter code and using as reference the H. Sapiens sequence) that are structurally close to or within functionally important regions of Ang protein and that are close (within 4Å) to coevolving pairs with potential compensatory relationships. In bold we highlight those co-evolving amino acid positions reported to be involved in dimmer formation of hAng, in Italic we remark positions implicated in the interaction with angiogenin-inhibitor in Human. We finally underscore those positions identified to be important as catalytic sites in hAng, as described in NCBI-IBIS database [78].

ISSN: 2730-7182