From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2feb.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2feb.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2feb| PDB=2feb | SCENE= }} | | {{STRUCTURE_2feb| PDB=2feb | SCENE= }} |
| | | | |
| - | '''NMR Solution Structure, Dynamics and Binding Properties of the Kringle IV Type 8 module of apolipoprotein(a)'''
| + | ===NMR Solution Structure, Dynamics and Binding Properties of the Kringle IV Type 8 module of apolipoprotein(a)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The plasma lipoprotein lipoprotein(a) [Lp(a)] comprises a low-density lipoprotein (LDL)-like particle covalently attached to the glycoprotein apolipoprotein(a) [apo(a)]. Apo(a) consists of multiple tandem repeating kringle modules, similar to plasminogen kringle IV (designated KIV1-KIV10), followed by modules homologous to the kringle V module and protease domain of plasminogen. The apo(a) KIV modules have been classified on the basis of their binding affinity for lysine and lysine analogues. The strong lysine-binding apo(a) KIV10 module mediates lysine-dependent interactions with fibrin and cell-surface receptors. Weak lysine-binding apo(a) KIV7 and KIV8 modules display a 2-3-fold difference in lysine affinity and play a direct role in the noncovalent step in Lp(a) assembly through binding to unique lysine-containing sequences in apolipoproteinB-100 (apoB-100). The present study describes the nuclear magnetic resonance solution structure of apo(a) KIV8 and its solution dynamics properties, the first for an apo(a) kringle module, and compares the effects of epsilon-aminocaproic acid (epsilon-ACA) binding on the backbone and side-chain conformation of KIV7 and KIV8 on a per residue basis. Apo(a) KIV8 adopts a well-ordered structure that shares the general tri-loop kringle topology with apo(a) KIV6, KIV7, and KIV10. Mapping of epsilon-ACA-induced chemical-shift changes on KIV7 and KIV8 indicate that the same residues are affected, despite a 2-3-fold difference in epsilon-ACA affinity. A unique loop conformation within KIV8, involving hydrophobic interactions with Tyr40, affects the positioning of Arg35 relative to the lysine-binding site (LBS). A difference in the orientation of the aromatic side chains comprising the hydrophobic center of the LBS in KIV8 decreases the size of the hydrophobic cleft compared to other apo(a) KIV modules. An exposed hydrophobic patch contiguous with the LBS in KIV8 and not conserved in other weak lysine-binding apo(a) kringle modules may modulate specificity for regions within apoB-100. An additional ligand recognition site comprises a structured arginine-glycine-aspartate motif at the N terminus of the KIV8 module, which may mediate Lp(a)/apo(a)-integrin interactions. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17263558}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17263558 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17263558}} |
| | | | |
| | ==Disease== | | ==Disease== |
| Line 19: |
Line 23: |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | 2FEB 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=2FEB OCA]. | + | 2FEB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEB OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 31: |
Line 35: |
| | [[Category: Disulphide bonded protein]] | | [[Category: Disulphide bonded protein]] |
| | [[Category: Tri-loop structure]] | | [[Category: Tri-loop structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:47:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:01:10 2008'' |
Revision as of 08:01, 28 July 2008
Template:STRUCTURE 2feb
NMR Solution Structure, Dynamics and Binding Properties of the Kringle IV Type 8 module of apolipoprotein(a)
Template:ABSTRACT PUBMED 17263558
Disease
Known disease associated with this structure: LPA deficiency, congenital OMIM:[152200], Coronary artery disease, susceptibility to OMIM:[152200]
About this Structure
2FEB is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
Nuclear magnetic resonance (NMR) solution structure, dynamics, and binding properties of the kringle IV type 8 module of apolipoprotein(a)., Chitayat S, Kanelis V, Koschinsky ML, Smith SP, Biochemistry. 2007 Feb 20;46(7):1732-42. Epub 2007 Jan 31. PMID:17263558
Page seeded by OCA on Mon Jul 28 11:01:10 2008
