3mtf
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:3mtf.jpg|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3mtf", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3mtf| PDB=3mtf | SCENE= }} | {{STRUCTURE_3mtf| PDB=3mtf | SCENE= }} | ||
| - | |||
===Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor=== | ===Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor=== | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_HUMAN]] Fibrodysplasia ossificans progressiva. Defects in ACVR1 are a cause of fibrodysplasia ossificans progressiva (FOP) [MIM:[http://omim.org/entry/135100 135100]]. FOP is a rare autosomal dominant disorder of skeletal malformations and progressive extraskeletal ossification. Heterotopic ossification in FOP begins in childhood and can be induced by trauma or may occur without warning. Bone formation is episodic and progressive, leading to extra-articular ankylosis of all major joints of the axial and appendicular skeleton, rendering movement impossible.<ref>PMID:16642017</ref> <ref>PMID:19085907</ref> <ref>PMID:19330033</ref> | ||
| + | |||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_HUMAN]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3mtf]] is a 2 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=3MTF OCA]. | |
| + | |||
| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Receptor protein serine/threonine kinase]] | [[Category: Receptor protein serine/threonine kinase]] | ||
| Line 40: | Line 38: | ||
[[Category: Structural genomics consortium]] | [[Category: Structural genomics consortium]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 23 08:52:24 2010'' | ||
Revision as of 21:17, 17 April 2013
Contents |
Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor
Disease
[ACVR1_HUMAN] Fibrodysplasia ossificans progressiva. Defects in ACVR1 are a cause of fibrodysplasia ossificans progressiva (FOP) [MIM:135100]. FOP is a rare autosomal dominant disorder of skeletal malformations and progressive extraskeletal ossification. Heterotopic ossification in FOP begins in childhood and can be induced by trauma or may occur without warning. Bone formation is episodic and progressive, leading to extra-articular ankylosis of all major joints of the axial and appendicular skeleton, rendering movement impossible.[1] [2] [3]
Function
[ACVR1_HUMAN] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin. May be involved for left-right pattern formation during embryogenesis (By similarity).
About this Structure
3mtf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Shore EM, Xu M, Feldman GJ, Fenstermacher DA, Cho TJ, Choi IH, Connor JM, Delai P, Glaser DL, LeMerrer M, Morhart R, Rogers JG, Smith R, Triffitt JT, Urtizberea JA, Zasloff M, Brown MA, Kaplan FS. A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. Nat Genet. 2006 May;38(5):525-7. Epub 2006 Apr 23. PMID:16642017 doi:ng1783
- ↑ Kaplan FS, Xu M, Seemann P, Connor JM, Glaser DL, Carroll L, Delai P, Fastnacht-Urban E, Forman SJ, Gillessen-Kaesbach G, Hoover-Fong J, Koster B, Pauli RM, Reardon W, Zaidi SA, Zasloff M, Morhart R, Mundlos S, Groppe J, Shore EM. Classic and atypical fibrodysplasia ossificans progressiva (FOP) phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1. Hum Mutat. 2009 Mar;30(3):379-90. doi: 10.1002/humu.20868. PMID:19085907 doi:10.1002/humu.20868
- ↑ Petrie KA, Lee WH, Bullock AN, Pointon JJ, Smith R, Russell RG, Brown MA, Wordsworth BP, Triffitt JT. Novel mutations in ACVR1 result in atypical features in two fibrodysplasia ossificans progressiva patients. PLoS One. 2009;4(3):e5005. doi: 10.1371/journal.pone.0005005. Epub 2009 Mar 30. PMID:19330033 doi:10.1371/journal.pone.0005005
Categories: Homo sapiens | Receptor protein serine/threonine kinase | Alfano, I. | Arrowsmith, C H. | Bountra, C. | Bullock, A. | Canning, P. | Chaikuad, A. | Cooper, C. | Daga, N. | Delft, F von. | Edwards, A M. | Knapp, S. | Krojer, T. | Mahajan, P. | Petrie, K. | SGC, Structural Genomics Consortium. | Sanvitale, C. | Vollmar, M. | Weigelt, J. | Protein kinase | Sgc | Structural genomic | Structural genomics consortium | Transferase
