Group:MUZIC:Enigma Family

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m
m
Line 1: Line 1:
=='''Enigma family: PDZ- and LIM-domain protein of the cytoskeleton'''==
=='''Enigma family: PDZ- and LIM-domain protein of the cytoskeleton'''==
-
'''Proteins''' within the enigma subfamily typically possess an N-terminal PDZ domain ('''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1) and at least one to three C-terminal LIM domain ('''L'''in-11, '''I'''sl1 and '''M'''ec-3) within their structure. Three major proteins have extensively been described and characterized within this subfamily: '''Enigma''', '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher/Oracle'''. These member proteins have all been located to the mammalian striated muscle, specifically in the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via thier LIM domain or internal motifs, for example ''ZM motif'' (ZASP motif), possibly to maintain the massive complex of interacting protein components of the muscle sarcomere for proper architecture and physiological function.
+
Three proteins have extensively been described and characterized within this subfamily: '''Enigma''', '''Enigma Homologue''' (ENH) protein and '''ZASP/Cypher''' ('ZASP' being the human orthologue of 'Cypher' which is found in mouse and also identified by independent researchers who named it 'Oracle').
 +
 
 +
Didactically, protein members of the enigma subfamily typically possess within their structure: '''(1)''' an N-terminal PDZ domain (a domain which is named after the first three proteins where it was initially characterized i.e. '''P'''SD 95, '''D'''isc large protein and '''Z'''onula Occludens 1), and '''(2)''' three C-terminal LIM domain (a domain which is named after the first three proteins where it was characterized i.e. '''L'''in-11, '''I'''sl1 and '''M'''ec-3) [[(1), (2)]].
 +
 
 +
The member proteins have all been located to the mammalian striated muscle, specifically in the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via thier LIM domain or internal motifs, for example ''ZM motif'' (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP).
 +
 
 +
These interactions via their PDZ- and LIM-domains have been suggested to be important for scaffolding interacting proteins in the sarcomere in order to maintain a proper architecture and physiologically functional muscle.
<Structure load='1wf7' size='350' frame='true' align='right' caption='NMR structure of the PDZ domain of ENH' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz_structure/1' />scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz_structure/1'>
<Structure load='1wf7' size='350' frame='true' align='right' caption='NMR structure of the PDZ domain of ENH' scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz_structure/1' />scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz_structure/1'>

Revision as of 14:33, 4 July 2011

Contents

Enigma family: PDZ- and LIM-domain protein of the cytoskeleton

Three proteins have extensively been described and characterized within this subfamily: Enigma, Enigma Homologue (ENH) protein and ZASP/Cypher ('ZASP' being the human orthologue of 'Cypher' which is found in mouse and also identified by independent researchers who named it 'Oracle').

Didactically, protein members of the enigma subfamily typically possess within their structure: (1) an N-terminal PDZ domain (a domain which is named after the first three proteins where it was initially characterized i.e. PSD 95, Disc large protein and Zonula Occludens 1), and (2) three C-terminal LIM domain (a domain which is named after the first three proteins where it was characterized i.e. Lin-11, Isl1 and Mec-3) (1), (2).

The member proteins have all been located to the mammalian striated muscle, specifically in the heart and skeletal muscle Z-disk. They interact via their PDZ domains with motor protein components of the Z-disk and also recruit signalling molecules via thier LIM domain or internal motifs, for example ZM motif (ZASP-like motif which is sandwiched between the PDZ- and LIM-domains in ZASP).

These interactions via their PDZ- and LIM-domains have been suggested to be important for scaffolding interacting proteins in the sarcomere in order to maintain a proper architecture and physiologically functional muscle.

NMR structure of the PDZ domain of ENH

Drag the structure with the mouse to rotate
scene='User:Adekunle_Onipe/workbench/Enigma_Family/Enh_pdz_structure/1'>


Enigma

Structure

Interactions within the Z-disk

Functions


Enigma Homologue (ENH)

Structure

Interaction within the Z-disk

Functions


ZASP/Cypher/Oracle

Structure

Interactions within the Z-disk

Functions



References

>

Proteopedia Page Contributors and Editors (what is this?)

Adekunle Onipe, Michal Harel

Personal tools