1EQY

COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1

Summary for 1EQY

• Entry DOI: 10.2210/pdb1eqy/pdb
• Descriptor: GELSOLIN, ALPHA ACTIN, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: gelsolin, actin, contractile protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 56798.26

Authors

McLaughlin, P.J.,Gooch, J.T.,Mannherz, H.G.,Weeds, A.G. (deposition date: 2000-04-06, release date: 2000-05-03, Last modification date: 2021-11-03)

Primary citation

McLaughlin, P.J.,Gooch, J.T.,Mannherz, H.G.,Weeds, A.G.
Structure of gelsolin segment 1-actin complex and the mechanism of filament severing.
Nature, 364:685-692, 1993

PubMed Abstract: The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.

PubMed: 8395021
DOI: 10.1038/364685a0

Experimental method

X-RAY DIFFRACTION (2.3 Å)