Group:MUZIC:XIN: Difference between revisions

Georg Mlynek (talk | contribs) No edit summary |
Georg Mlynek (talk | contribs) No edit summary |
||
Line 3: | Line 3: | ||
{{TOC limit|limit=2}} | {{TOC limit|limit=2}} | ||
== Sequence Annotation == | == Sequence Annotation == | ||
[[Image:3hop.png|left|200px|thumb|Crystal structure of Human Filamin A, [[3hop]]]] | |||
{{STRUCTURE_3hop| PDB=3hop | SIZE=300| SCENE=Filamin/Cv/1 |right|CAPTION=Human Filamin A, [[3hop]] }} | |||
[[Filamin]] '''A (FLNA)''' has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins. '''Filamin B (FLNB)''' is a human cytoplasmic protein which functions similarly to FLNA and guides proper skeletal development. '''Filamin C (FLNC)''' is functionally similar and contains 3 domains: the N-terminal ABD, the C-terminal dimerization domain (DD) and a membrane glycoprotein-binding domain. The images at the left and at the right correspond to one representative filamin structure, ''i.e.'' the crystal structure of human filamin A ([[3hop]]), it forms a <scene name='Filamin/Cv/2'>dimer</scene> <ref>PMID:19773341</ref>. Two phosphate ions are rendered as space filling objects. | |||
{{TOC limit|limit=2}} | |||
== Filamin A == | |||
Revision as of 11:14, 5 July 2011
Xin actin-binding repeat-containing protein 1 (Alternative name: Cardiomyopathy-associated protein 1) is coded by the gene (Synonyms:CMYA1, XIN) and has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins.
Sequence AnnotationSequence Annotation
Template:STRUCTURE 3hop Filamin A (FLNA) has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins. Filamin B (FLNB) is a human cytoplasmic protein which functions similarly to FLNA and guides proper skeletal development. Filamin C (FLNC) is functionally similar and contains 3 domains: the N-terminal ABD, the C-terminal dimerization domain (DD) and a membrane glycoprotein-binding domain. The images at the left and at the right correspond to one representative filamin structure, i.e. the crystal structure of human filamin A (3hop), it forms a [1]. Two phosphate ions are rendered as space filling objects.
Filamin AFilamin A
3isw – hFLNA repeat 21+CFTR peptide – human
2wfn, 3hop, 3hor – hFLNA ABD
3hoc – hFLNA ABD (mutant)
FunctionFunction
Interactions with other proteinsInteractions with other proteins
Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">.
Clinical significanceClinical significance
1wlh, 1qfh – FLN rod domain – Dictyostelium discoideum
ReferencesReferences
- ↑ Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. Hum Mol Genet. 2009 Dec 15;18(24):4791-800. Epub 2009 Sep 22. PMID:19773341 doi:10.1093/hmg/ddp442
- ↑ Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. Hum Mol Genet. 2009 Dec 15;18(24):4791-800. Epub 2009 Sep 22. PMID:19773341 doi:10.1093/hmg/ddp442
ReferencesReferences