2AO7

Adam10 Disintegrin and cysteine- rich domain

Summary for 2AO7

• Entry DOI: 10.2210/pdb2ao7/pdb
• Descriptor: ADAM 10, SULFATE ION (2 entities in total)
• Functional Keywords: extracellular, protease, disintegrin, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Golgi apparatus membrane; Single-pass type I membrane protein: Q10741
• Total number of polymer chains: 1
• Total formula weight: 21062.79

Authors

Janes, P.W.,Saha, N.,Barton, W.A.,Kolev, M.V.,Wimmer-Kleikamp, S.H.,Nievergall, E.,Blobel, C.P.,Himanen, J.-P.,Lackmann, M.,Nikolov, D.B. (deposition date: 2005-08-12, release date: 2006-08-08, Last modification date: 2024-12-25)

Primary citation

Janes, P.W.,Saha, N.,Barton, W.A.,Kolev, M.V.,Wimmer-Kleikamp, S.H.,Nievergall, E.,Blobel, C.P.,Himanen, J.-P.,Lackmann, M.,Nikolov, D.B.
Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.
Cell(Cambridge,Mass.), 123:291-304, 2005

PubMed Abstract: Ephrin ligands presented on one cell surface associate with their receptors on the surface of a juxtaposed cell, often resulting in cell-cell repulsion. In this issue of Cell, Janes et al. (2005) show that the ephrin ligand can be proteolytically released from its membrane tether by a complex on the opposing cell composed of the ephrin receptor and an ADAM metalloprotease.

PubMed: 16239135
DOI: 10.1016/j.cell.2005.08.014

Experimental method

X-RAY DIFFRACTION (2.9 Å)