This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1sra
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The EF-hand is a highly conserved Ca(2+)-binding motif found in many | + | The EF-hand is a highly conserved Ca(2+)-binding motif found in many cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair. The two EF-hands interact canonically but their detailed structures are unusual. In the first EF-hand a one-residue insertion is accommodated by a cis-peptide bond and by substituting a carboxylate by a peptide carbonyl as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond. The EF-hand pair interacts tightly with an amphiphilic amino-terminal helix, reminiscent of target peptide binding by calmodulin. The present structure defines a novel protein module occurring in several other extracellular proteins. |
==About this Structure== | ==About this Structure== | ||
| Line 16: | Line 16: | ||
[[Category: Hohenadl, C.]] | [[Category: Hohenadl, C.]] | ||
[[Category: Hohenester, E.]] | [[Category: Hohenester, E.]] | ||
| - | [[Category: Jansonius, J | + | [[Category: Jansonius, J N.]] |
[[Category: Maurer, P.]] | [[Category: Maurer, P.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
| Line 22: | Line 22: | ||
[[Category: extracellular matrix protein]] | [[Category: extracellular matrix protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:25 2008'' |
Revision as of 13:04, 21 February 2008
|
STRUCTURE OF A NOVEL EXTRACELLULAR CA2+-BINDING MODULE IN BM-40(SLASH)SPARC(SLASH)OSTEONECTIN
Overview
The EF-hand is a highly conserved Ca(2+)-binding motif found in many cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair. The two EF-hands interact canonically but their detailed structures are unusual. In the first EF-hand a one-residue insertion is accommodated by a cis-peptide bond and by substituting a carboxylate by a peptide carbonyl as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond. The EF-hand pair interacts tightly with an amphiphilic amino-terminal helix, reminiscent of target peptide binding by calmodulin. The present structure defines a novel protein module occurring in several other extracellular proteins.
About this Structure
1SRA is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a novel extracellular Ca(2+)-binding module in BM-40., Hohenester E, Maurer P, Hohenadl C, Timpl R, Jansonius JN, Engel J, Nat Struct Biol. 1996 Jan;3(1):67-73. PMID:8548457
Page seeded by OCA on Thu Feb 21 15:04:25 2008
