1whf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1whf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1whf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1whf| PDB=1whf | SCENE= }}
{{STRUCTURE_1whf| PDB=1whf | SCENE= }}
-
'''COAGULATION FACTOR, NMR, 15 STRUCTURES'''
+
===COAGULATION FACTOR, NMR, 15 STRUCTURES===
-
==Overview==
+
<!--
-
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).
+
The line below this paragraph, {{ABSTRACT_PUBMED_8794734}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8794734 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8794734}}
==About this Structure==
==About this Structure==
-
1WHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WHF OCA].
+
1WHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WHF OCA].
==Reference==
==Reference==
Line 34: Line 38:
[[Category: Plasma]]
[[Category: Plasma]]
[[Category: Serine protease]]
[[Category: Serine protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:40:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:22:11 2008''

Revision as of 13:22, 29 July 2008

Template:STRUCTURE 1whf

COAGULATION FACTOR, NMR, 15 STRUCTURES

Template:ABSTRACT PUBMED 8794734

About this Structure

1WHF is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

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., Sunnerhagen M, Olah GA, Stenflo J, Forsen S, Drakenberg T, Trewhella J, Biochemistry. 1996 Sep 10;35(36):11547-59. PMID:8794734

Page seeded by OCA on Tue Jul 29 16:22:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools