 |
PDBsum entry 1by2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Extracellular module
|
PDB id
|
|
|
|
1by2
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of a scavenger receptor cysteine-Rich domain sheds light on an ancient superfamily.
|
|
|
Authors
|
|
E.Hohenester,
T.Sasaki,
R.Timpl.
|
|
|
Ref.
|
|
Nat Struct Biol, 1999,
6,
228-232.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Scavenger receptor cysteine-rich (SRCR) domains are found widely in cell surface
molecules and in some secreted proteins, where they are thought to mediate
ligand binding. We have determined the crystal structure at 2.0 A resolution of
the SRCR domain of Mac-2 binding protein (M2BP), a tumor-associated antigen and
matrix protein. The structure reveals a curved six-stranded beta-sheet cradling
an alpha-helix. Structure-based sequence alignment demonstrates that the M2BP
SRCR domain is a valid template for the entire SRCR protein superfamily. This
allows an interpretation of previous mutagenesis data on ligand binding to the
lymphocyte receptor CD6.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Two orthogonal views^32 of the M2BP SRCR domain
structure.  -strands
are in green and are labeled sequentially A−F; the  -helix
is in pink. Disulfide bridges are in yellow and the sequence
numbers of cysteine residues are indicated.
|
|
Figure 4.
Figure 4. Stereo view of the experimental electron density map
after solvent flattening at 3.0 Å resolution. The map
is contoured at the 1.0  level
and the final refined model is superimposed on the map. Shown is
the region around -strand
B and the B−C hairpin. Made with BOBSCRIPT^33.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
228-232)
copyright 1999.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Mac-2 binding protein is a cell-Adhesive protein of the extracellular matrix which self-Assembles into ring-Like structures and binds beta1 integrins, Collagens and fibronectin.
|
|
|
Authors
|
|
T.Sasaki,
C.Brakebusch,
J.Engel,
R.Timpl.
|
|
|
Ref.
|
|
Embo J, 1998,
17,
1606-1613.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 2.
Figure 2 Ring-like aggregates of M2BP in PBS, pH 7.4, visualized
by electron microscopy after rotary shadowing (A) and negative
staining at neutral pH (B). The rotary shadowing technique
reveals dissociation of the rings in 0.1 M acetic acid (C). Bar,
100 nm.
|
|
Figure 7.
Figure 7 Double immunofluorescence staining for M2BP and nidogen
on frozen mouse tissue sections. The tissues used were testis
(A), spleen (B), thymus (C) and skeletal muscle (D). Staining
was with a rat monoclonal antibody against mouse nidogen and the
affinity-purified rabbit antibody against M2BP. Control refers
to a similar section treated with normal rabbit IgG for the
evaluation of background binding. Bar, 100  m.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
which is an Open Access publication published by Macmillan Publishers Ltd
|
|
|
Secondary reference #2
|
|
|
Title
|
|
The srcr superfamily: a family reminiscent of the ig superfamily.
|
|
|
Authors
|
|
D.Resnick,
A.Pearson,
M.Krieger.
|
|
|
Ref.
|
|
Trends Biochem Sci, 1994,
19,
5-8.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
