2vx3: Difference between revisions
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{{STRUCTURE_2vx3| PDB=2vx3 | SCENE= }} | {{STRUCTURE_2vx3| PDB=2vx3 | SCENE= }} | ||
===Crystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1A=== | |||
{{ABSTRACT_PUBMED_021126318}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/DYR1A_HUMAN DYR1A_HUMAN]] Defects in DYRK1A are the cause of mental retardation autosomal dominant type 7 (MRD7) [MIM:[http://omim.org/entry/614104 614104]]. A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period.<ref>PMID:21294719</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/DYR1A_HUMAN DYR1A_HUMAN]] May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates.<ref>PMID:8769099</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[2vx3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VX3 OCA]. | [[2vx3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VX3 OCA]. | ||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: Dual-specificity kinase]] | [[Category: Dual-specificity kinase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 06:47, 25 March 2013
Crystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1ACrystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1A
Template:ABSTRACT PUBMED 021126318
DiseaseDisease
[DYR1A_HUMAN] Defects in DYRK1A are the cause of mental retardation autosomal dominant type 7 (MRD7) [MIM:614104]. A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period.[1]
FunctionFunction
[DYR1A_HUMAN] May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates.[2]
About this StructureAbout this Structure
2vx3 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ van Bon BW, Hoischen A, Hehir-Kwa J, de Brouwer AP, Ruivenkamp C, Gijsbers AC, Marcelis CL, de Leeuw N, Veltman JA, Brunner HG, de Vries BB. Intragenic deletion in DYRK1A leads to mental retardation and primary microcephaly. Clin Genet. 2011 Mar;79(3):296-9. doi: 10.1111/j.1399-0004.2010.01544.x. PMID:21294719 doi:10.1111/j.1399-0004.2010.01544.x
- ↑ Shindoh N, Kudoh J, Maeda H, Yamaki A, Minoshima S, Shimizu Y, Shimizu N. Cloning of a human homolog of the Drosophila minibrain/rat Dyrk gene from "the Down syndrome critical region" of chromosome 21. Biochem Biophys Res Commun. 1996 Aug 5;225(1):92-9. PMID:8769099 doi:S0006-291X(96)91135-3
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OCA- Dual-specificity kinase
- Homo sapiens
- Arrowsmith, C H.
- Bountra, C.
- Burgess-Brown, N.
- Delft, F Von.
- Edwards, A.
- Fedorov, O.
- Filippakopoulos, P.
- King, O.
- Knapp, S.
- Philips, C.
- Pike, A C.W.
- Roos, A K.
- Soundararajan, M.
- Wikstrom, M.
- Casp8
- Kinase
- Minibrain homolog
- Nucleotide-binding
- Phosphoprotein
- Serine/threonine-protein kinase
- Transferase
- Tyrosine-protein kinase