 |
PDBsum entry 1whf
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
The relative orientation of gla and egf domains in coagulation factor X is altered by ca2+ binding to the first egf domain. A combined nmr-Small angle X-Ray scattering study.
|
|
|
Authors
|
|
M.Sunnerhagen,
G.A.Olah,
J.Stenflo,
S.Forsén,
T.Drakenberg,
J.Trewhella.
|
|
|
Ref.
|
|
Biochemistry, 1996,
35,
11547-11559.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Coagulation factor X is a serine protease containing three noncatalytic domains:
an N-terminal gamma-carboxyglutamic acid (Gla)1 domain followed by two epidermal
growth factor (EGF)-like domains. The isolated N-terminal EGF domain binds Ca2+
with a Kd of 10(-3) M. When linked to the Gla domain, however, its Ca2+ affinity
is increased 10-fold. In this paper, we present the NMR solution structure of
the factor X Gla-EGF domain pair with Ca2+ bound to the EGF domain, as well as
small angle X-ray scattering (SAXS) data on the Gla-EGF domain pair with and
without Ca2+. Our results show that Ca2+ binding to the EGF domain makes the Gla
and EGF domains fold toward each other using the Ca2+ site as a hinge.
Presumably, a similar mechanism may be responsible for alterations in the
relative orientation of protein domains in many other extracellular proteins
containing EGF domains with the consensus for Ca2+ binding. The results of the
NMR and SAXS measurements reported in this paper confirm our previous result
that the Gla domain is folded also in its apo state when linked to the EGF
domain [Sunnerhagen, M., et al. (1995) Nat. Struct. Biol. 2, 504-509]. Finally,
our study clearly demonstrates the powerful combination of NMR and SAXS in the
study of modular proteins, since this enables reliable evaluation of both
short-range (NMR) and long-range interactions (SAXS).
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Structure of the ca(2+)-Free gla domain sheds light on membrane binding of blood coagulation proteins.
|
|
|
Authors
|
|
M.Sunnerhagen,
S.Forsén,
A.M.Hoffrén,
T.Drakenberg,
O.Teleman,
J.Stenflo.
|
|
|
Ref.
|
|
Nat Struct Biol, 1995,
2,
504-509.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
How an epidermal growth factor (egf)-Like domain binds calcium. High resolution nmr structure of the calcium form of the nh2-Terminal egf-Like domain in coagulation factor X.
|
|
|
Authors
|
|
M.Selander-Sunnerhagen,
M.Ullner,
E.Persson,
O.Teleman,
J.Stenflo,
T.Drakenberg.
|
|
|
Ref.
|
|
J Biol Chem, 1992,
267,
19642-19649.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Three-Dimensional structure of the apo form of the n-Terminal egf-Like module of blood coagulation factor X as determined by nmr spectroscopy and simulated folding.
|
|
|
Authors
|
|
M.Ullner,
M.Selander,
E.Persson,
J.Stenflo,
T.Drakenberg,
O.Teleman.
|
|
|
Ref.
|
|
Biochemistry, 1992,
31,
5974-5983.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
