2xqn | pdb_00002xqn
COMPLEX OF THE 2ND AND 3RD LIM DOMAINS OF TES WITH THE EVH1 DOMAIN OF MENA AND THE N-TERMINAL DOMAIN OF ACTIN-LIKE PROTEIN ARP7A
Structural highlights
Function[TES_HUMAN] Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth.[1] [2] [3] [ENAH_HUMAN] Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity).[4] [5] Publication Abstract from PubMedActin related proteins (Arps) are a highly conserved family of proteins that have extensive sequence and structural similarity to actin. All characterized Arps are components of large multimeric complexes associated with chromatin or the cytoskeleton. In addition, the human genome encodes five conserved but largely uncharacterized orphan Arps, which appear to be mostly testis specific. Here we show that Arp7A, which has 43% sequence identity with beta-actin, forms a complex with the cytoskeletal proteins Tes and Mena in the subacrosomal layer of round spermatids. The N-terminal 65 residue extension to the actin-like fold of Arp7A interacts directly with Tes. The crystal structure of the 1-65Arp7A:LIM2-3Tes:EVH1Mena complex reveals that residues 28 - 49 of Arp7A contact the LIM2-3 domains of Tes. Two alanine residues from Arp7A that occupy equivalent apolar pockets in both LIM domains as well as an intervening GPAK linker that binds the LIM2-3 junction, are critical for the Arp7A:Tes interaction. Equivalent occupied apolar pockets are also seen in the tandem LIM domain structures of LMO4 and Lhx3 bound to unrelated ligands. Our results indicate that apolar pocket interactions are a common feature of tandem LIM domain interactions, but ligand specificity is principally determined by the linker sequence. Molecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7A.,Boeda B, Knowles PP, Briggs D, Murray-Rust J, Soriano E, Garvalov BK, McDonald NQ, Way M J Biol Chem. 2011 Jan 29. PMID:21278383[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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