1i8n
From Proteopedia
(New page: 200px<br /><applet load="1i8n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8n, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1i8n.jpg|left|200px]]<br /><applet load="1i8n" size=" | + | [[Image:1i8n.jpg|left|200px]]<br /><applet load="1i8n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i8n, resolution 2.2Å" /> | caption="1i8n, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF LEECH ANTI-PLATELET PROTEIN'''<br /> | '''CRYSTAL STRUCTURE OF LEECH ANTI-PLATELET PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Leech anti-platelet protein (LAPP) from the leech Haementeria officinalis | + | Leech anti-platelet protein (LAPP) from the leech Haementeria officinalis is a collagen-binding protein that inhibits the collagen-mediated adhesion of blood platelets. The crystal structure of recombinant LAPP has been determined using single isomorphous replacement with anomalous scattering combined with solvent flattening and threefold molecular averaging. The model of LAPP has been refined to 2.2 A resolution (R factor 21.5%; free R factor 24.0%). LAPP contains an 89-residue C-terminal domain consisting of a central six-stranded antiparallel beta-sheet flanked on one side by an alpha-helix and on the other side by two extended loops with little secondary structure. A 36-residue N-terminal region is not visible in the electron-density map. This region is rich in glycine and lacks hydrophobic residues. It probably does not have a compact globular fold, but instead has an extended conformation and is flexible. The crystal packing suggests that LAPP may form tightly interacting dimers. The fold of the C-terminal domain of LAPP closely resembles that of the N-domain of hepatocyte growth factor (HGF), which classifies LAPP as a PAN domain. However, no significant sequence homology exists between LAPP and other PAN domains. Common structural features between LAPP and the HGF N-domain include two disulfide bonds that link the alpha-helix to the central region of the protein and five residues with a conserved hydrophobic nature that are located in the core of the domain. These conserved structural features may be an important determinant of the PAN-domain type of fold. |
==About this Structure== | ==About this Structure== | ||
| - | 1I8N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haementeria_officinalis Haementeria officinalis] with ROP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1I8N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haementeria_officinalis Haementeria officinalis] with <scene name='pdbligand=ROP:'>ROP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haementeria officinalis]] | [[Category: Haementeria officinalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Connolly, T | + | [[Category: Connolly, T M.]] |
[[Category: Gros, P.]] | [[Category: Gros, P.]] | ||
| - | [[Category: Huizinga, E | + | [[Category: Huizinga, E G.]] |
[[Category: Kroon, J.]] | [[Category: Kroon, J.]] | ||
[[Category: Schouten, A.]] | [[Category: Schouten, A.]] | ||
| - | [[Category: Sixma, J | + | [[Category: Sixma, J J.]] |
[[Category: ROP]] | [[Category: ROP]] | ||
[[Category: pan module]] | [[Category: pan module]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:14 2008'' |
Revision as of 11:09, 21 February 2008
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CRYSTAL STRUCTURE OF LEECH ANTI-PLATELET PROTEIN
Overview
Leech anti-platelet protein (LAPP) from the leech Haementeria officinalis is a collagen-binding protein that inhibits the collagen-mediated adhesion of blood platelets. The crystal structure of recombinant LAPP has been determined using single isomorphous replacement with anomalous scattering combined with solvent flattening and threefold molecular averaging. The model of LAPP has been refined to 2.2 A resolution (R factor 21.5%; free R factor 24.0%). LAPP contains an 89-residue C-terminal domain consisting of a central six-stranded antiparallel beta-sheet flanked on one side by an alpha-helix and on the other side by two extended loops with little secondary structure. A 36-residue N-terminal region is not visible in the electron-density map. This region is rich in glycine and lacks hydrophobic residues. It probably does not have a compact globular fold, but instead has an extended conformation and is flexible. The crystal packing suggests that LAPP may form tightly interacting dimers. The fold of the C-terminal domain of LAPP closely resembles that of the N-domain of hepatocyte growth factor (HGF), which classifies LAPP as a PAN domain. However, no significant sequence homology exists between LAPP and other PAN domains. Common structural features between LAPP and the HGF N-domain include two disulfide bonds that link the alpha-helix to the central region of the protein and five residues with a conserved hydrophobic nature that are located in the core of the domain. These conserved structural features may be an important determinant of the PAN-domain type of fold.
About this Structure
1I8N is a Single protein structure of sequence from Haementeria officinalis with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of leech anti-platelet protein, an inhibitor of haemostasis., Huizinga EG, Schouten A, Connolly TM, Kroon J, Sixma JJ, Gros P, Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1071-8. Epub 2001, Jul 23. PMID:11468390
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