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PROSITE documentation PDOC00297 [for PROSITE entry PS51263] |
The actin-depolymerizing factor homology (ADF-H) domain is an ~150-amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins [1,2,3]:
Although these proteins are biochemically distinct and play different roles in actin dynamics, they all appear to use the ADF-H domain for their interactions with actin.
The ADF-H domain consists of a six-stranded mixed β-sheet in which the four central strands (β2-β5) are anti-parallel and the two edge strands (β1 and β6) run parallel with the neighboring strands. The sheet is surrounded by two α-helices on each side (see <PDB:1COF>) [1,2,4].
The profile we developed covers the entire ADF-H domain.
Last update:October 2006 / Pattern removed, profile added and text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Lappalainen P. Kessels M.M. Cope M.J. Drubin D.G. |
Title | The ADF homology (ADF-H) domain: a highly exploited actin-binding module. | |
Source | Mol. Biol. Cell 9:1951-1959(1998). | |
PubMed ID | 9693358 |
2 | Authors | Paavilainen V.O. Merckel M.C. Falck S. Ojala P.J. Pohl E. Wilmanns M. Lappalainen P. |
Title | Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin. | |
Source | J. Biol. Chem. 277:43089-43095(2002). | |
PubMed ID | 12207032 | |
DOI | 10.1074/jbc.M208225200 |
3 | Authors | Liu L.X. Xu H. Weller P.F. Shi A. Debnath I. |
Title | Structure and expression of a novel filarial gene for glia maturation factor. | |
Source | Gene 186:1-5(1997). | |
PubMed ID | 9047337 |
4 | Authors | Liu L. Wei Z. Wang Y. Wan M. Cheng Z. Gong W. |
Title | Crystal structure of human coactosin-like protein. | |
Source | J. Mol. Biol. 344:317-323(2004). | |
PubMed ID | 15522287 | |
DOI | 10.1016/j.jmb.2004.09.036 |