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PDBsum entry 2ao7
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Adam10 disintegrin and cysteine- rich domain
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Structure:
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Adam 10. Chain: a. Synonym: a disintegrin and metalloproteinase domain 10, mammalian disintegrin-metalloprotease, myelin-associated metalloproteinase, kuzbanian protein homolog. Engineered: yes
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Source:
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Bos taurus. Cattle. Organism_taxid: 9913. Gene: adam10, madm. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293
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Resolution:
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2.90Å
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R-factor:
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0.261
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R-free:
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0.289
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Authors:
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P.W.Janes,N.Saha,W.A.Barton,M.V.Kolev,S.H.Wimmer-Kleikamp, E.Nievergall,C.P.Blobel,J.-P.Himanen,M.Lackmann,D.B.Nikolov
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Key ref:
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F.Mancia
and
L.Shapiro
(2005).
ADAM and Eph: how Ephrin-signaling cells become detached.
Cell,
123,
185-187.
PubMed id:
DOI:
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Date:
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12-Aug-05
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Release date:
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08-Aug-06
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PROCHECK
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Headers
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References
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Q10741
(ADA10_BOVIN) -
Disintegrin and metalloproteinase domain-containing protein 10 from Bos taurus
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Seq:
Struc:
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748 a.a.
146 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.4.24.81
- ADAM10 endopeptidase.
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Cofactor:
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Zn(2+)
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DOI no:
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Cell
123:185-187
(2005)
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PubMed id:
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ADAM and Eph: how Ephrin-signaling cells become detached.
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F.Mancia,
L.Shapiro.
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ABSTRACT
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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.
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Selected figure(s)
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Figure 1.
Figure 1. The Association between the ADAM10 Protease and
the Ephrin-A5/EphA3 Ligand-Receptor Signaling Complex
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The above figure is
reprinted
by permission from Cell Press:
Cell
(2005,
123,
185-187)
copyright 2005.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Salaita,
and
J.T.Groves
(2010).
Roles of the cytoskeleton in regulating EphA2 signals.
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Commun Integr Biol,
3,
454-457.
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T.Tousseyn,
A.Thathiah,
E.Jorissen,
T.Raemaekers,
U.Konietzko,
K.Reiss,
E.Maes,
A.Snellinx,
L.Serneels,
O.Nyabi,
W.Annaert,
P.Saftig,
D.Hartmann,
and
B.De Strooper
(2009).
ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase.
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J Biol Chem,
284,
11738-11747.
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L.Shapiro,
J.Love,
and
D.R.Colman
(2007).
Adhesion molecules in the nervous system: structural insights into function and diversity.
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Annu Rev Neurosci,
30,
451-474.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
