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1dqb
From Proteopedia
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[[Image:1dqb.gif|left|200px]] | [[Image:1dqb.gif|left|200px]] | ||
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'''NMR STRUCTURE OF THROMBOMODULIN EGF(4-5)''' | '''NMR STRUCTURE OF THROMBOMODULIN EGF(4-5)''' | ||
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[[Category: Sampoli-Benitez, B A.]] | [[Category: Sampoli-Benitez, B A.]] | ||
[[Category: Wood, M J.]] | [[Category: Wood, M J.]] | ||
| - | [[Category: | + | [[Category: Anticoagulant]] |
| - | [[Category: | + | [[Category: Egf module]] |
| - | [[Category: | + | [[Category: Glycosylation]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Thrombin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:08:59 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:09, 2 May 2008
NMR STRUCTURE OF THROMBOMODULIN EGF(4-5)
Overview
A glycosylated fragment of thrombomodulin containing two epidermal growth factor-like domains (TMEGF45) was analyzed by NMR. The 4th-domains structure of this two-domain fragment is similar to that of the individual domain previously determined. The 5th-domain, which has uncrossed disulfide bonds, is not as well determined in the two-domain fragment than the individual domain previously solved. The flexibility of the 5th-domain is consistent with low heteronuclear NOEs. In the individual 5th-domain, Met 388 was disordered, and key thrombin binding residues formed a hydrophobic core. By contrast, in TMEGF45, Met 388 is in the 5th-domain core, positioned by Phe 376 from the 4th-domain. As a result, key thrombin binding residues that were in the core of the individual domain are expelled. Upon thrombin binding, chemical shifts of two residues in the 4th-domain, the three interdomain linker residues, and nearly all of the 5th-domain are perturbed. Thus, TMEGF45 binds thrombin by an induced fit mechanism involving a flexible 5th-domain.
About this Structure
1DQB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the smallest cofactor-active fragment of thrombomodulin., Wood MJ, Sampoli Benitez BA, Komives EA, Nat Struct Biol. 2000 Mar;7(3):200-4. PMID:10700277 Page seeded by OCA on Fri May 2 14:08:59 2008
