PMID- 10404224
OWN - NLM
STAT- MEDLINE
DCOM- 19990806
LR  - 20131121
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 6
IP  - 7
DP  - 1999 Jul
TI  - Structure of EVH1, a novel proline-rich ligand-binding module involved in
      cytoskeletal dynamics and neural function.
PG  - 661-5
AB  - The Ena-VASP homology (EVH1) domain is a protein interaction module found in
      several proteins that are involved in transducing migratory and morphological
      signals into cytoskeletal reorganization. EVH1 specifically recognizes
      proline-rich sequences in its binding partners and directs the localization and
      formation of multicomponent assemblies involved in actin-based motile processes
      and neural development. The structure of the complex between an EVH1 domain and
      the target peptide sequence EFPPPPT identifies the interactions responsible for
      recognition and distinguishes it from other proline-rich binding modules,
      including SH3 and WW domains. Surprisingly, the EVH1 domain has structural
      similarity to pleckstrin homology (PH), phosphotyrosine-binding (PTB) and
      ran-binding (RanBD) domains.
FAU - Fedorov, A A
AU  - Fedorov AA
AD  - Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 
      10461, USA.
FAU - Fedorov, E
AU  - Fedorov E
FAU - Gertler, F
AU  - Gertler F
FAU - Almo, S C
AU  - Almo SC
LA  - eng
SI  - PDB/1QC6
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 9DLQ4CIU6V (Proline)
SB  - IM
MH  - Amino Acid Sequence
MH  - Crystallography, X-Ray
MH  - Cytoskeleton/*chemistry
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Neurons/*chemistry
MH  - Proline/*chemistry
MH  - Protein Structure, Secondary
MH  - *Protein Structure, Tertiary
MH  - Sequence Homology, Amino Acid
MH  - src Homology Domains
EDAT- 1999/07/15 10:00
MHDA- 2001/03/23 10:01
CRDT- 1999/07/15 10:00
PHST- 1999/07/15 10:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/07/15 10:00 [entrez]
AID - 10.1038/10717 [doi]
PST - ppublish
SO  - Nat Struct Biol. 1999 Jul;6(7):661-5. doi: 10.1038/10717.