Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
Prehoda, K E
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. [electronic resource] - Cell May 1999 - 471-80 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0092-8674
10.1016/s0092-8674(00)80757-6 doi
Actins--metabolism
Amino Acid Sequence
Animals
Binding Sites
Cell Adhesion Molecules--chemistry
DNA-Binding Proteins--chemistry
Humans
Microfilament Proteins
Molecular Sequence Data
Peptides--chemistry
Phosphoproteins--chemistry
Protein Conformation
Proteins--chemistry
Sequence Homology, Amino Acid
Structure-Activity Relationship
Wiskott-Aldrich Syndrome Protein
Vasodilator-Stimulated Phosphoprotein
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. [electronic resource] - Cell May 1999 - 471-80 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0092-8674
10.1016/s0092-8674(00)80757-6 doi
Actins--metabolism
Amino Acid Sequence
Animals
Binding Sites
Cell Adhesion Molecules--chemistry
DNA-Binding Proteins--chemistry
Humans
Microfilament Proteins
Molecular Sequence Data
Peptides--chemistry
Phosphoproteins--chemistry
Protein Conformation
Proteins--chemistry
Sequence Homology, Amino Acid
Structure-Activity Relationship
Wiskott-Aldrich Syndrome Protein
Vasodilator-Stimulated Phosphoprotein