Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
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The SH3 domain of a M7 interacts with its C-terminal proline-rich regionCalmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative chargeEvidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosinsIntramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.An experimentally based computer search identifies unstructured membrane-binding sites in proteins: application to class I myosins, PAKS, and CARMIL
P2860
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 09 August 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@en
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
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type
label
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@en
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@nl
prefLabel
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@en
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@nl
P2093
P2860
P356
P1476
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
@en
P2093
Alasdair C Steven
Edward D Korn
Naiqian Cheng
Takashi Ishikawa
P2860
P304
12189-12194
P356
10.1073/PNAS.0404835101
P407
P577
2004-08-09T00:00:00Z