Crystallization (Comment) | Organism |
---|---|
JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D939R | the mutation increases the Kd of JMJD2A for H4K20me3 by about 200fold but does not markedly change the affinity for H3K4me3 | Homo sapiens |
D945R | the mutation increases the Kd of JMJD2A for H3K4me3 by about 200fold, but does not affect the interaction with H4K20me3 | Homo sapiens |
H18G | the mutation increases the Kd for H3K4me3 by fivefold compared to the wild-type enzyme | Homo sapiens |
N940R | the mutation does not perturb JMJD2A binding to H4K20me3 but decreases its affinity for H3K4me3 by about 46fold | Homo sapiens |
T968A | the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3 | Homo sapiens |
T968R | the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3 | Homo sapiens |
Y942A | the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3 | Homo sapiens |
Y942R | the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3 | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Kd values for H3K4me3 peptide with wild-type and mutant enzymes, overview | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2 | Homo sapiens | - |
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O75164 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | JMJD2A also demethylates histone H3 dimethylated or trimethylated at lysine 9 and lysine 36, by means of an N-terminal catalytic domain, as well as peptides from H4K20me3, recognized through its tudor domains. The hybrid tudor domains at the C terminus of JMJD2A are necessary for the demethylation activity of JMJD2A in vivo. H3K4me3 and H4K20me3 are recognized with similar affinities by JMJD2A, binding structures, overview. Two other amino acids of JMJD2A, Tyr942 and Thr968, involved in weaker intermolecular hydrogen bonds, selectively contact one peptide and not the other. The hydroxyl group of Thr968 in the wild-type structure forms a hydrogen bond with the guanido group of H4K20me3 Arg23 but does not contact H3K4me3. Tyr942 and Thr968 are not essential for the tight binding of JMJD2A to H3K4me3 and H4K20me3 | Homo sapiens | ? | - |
? | |
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2 | - |
Homo sapiens | [histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2 | - |
? | |
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2 | JMJD2A has the unique property of binding trimethylated peptides from histone sequences, H3K4me3 through itstandem hybrid tudor domains. JMJD2A Asp945 and Asp940 interact with Arg2 of the H3K4me3 peptide, but not with H4K20me3. Asn940 forms hydrogen bonds with the backbone amide and hydroxyl groups of H3K4me3 Thr3 | Homo sapiens | [histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the hybrid tudor domains at the C terminus of JMJD2A are necessary for the demethylation activity of JMJD2A in vivo | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
JMJD2A | - |
Homo sapiens |
JMJD2A-tudor | - |
Homo sapiens |
lysine demethylase | - |
Homo sapiens |