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)''' | + | {{Structure |
| + | |PDB= 1dqb |SIZE=350|CAPTION= <scene name='initialview01'>1dqb</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR STRUCTURE OF THROMBOMODULIN EGF(4-5)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DQB is a [ | + | 1DQB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQB OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10700277 10700277] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thrombin]] | [[Category: thrombin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:34 2008'' |
Revision as of 08:42, 20 March 2008
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NMR STRUCTURE OF THROMBOMODULIN EGF(4-5)
Contents |
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.
Disease
Known diseases associated with this structure: Myocardial infarction, susceptibility to OMIM:[188040], Thrombophilia due to thrombomodulin defect OMIM:[188040]
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 Thu Mar 20 10:42:34 2008
