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From Proteopedia
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'''5IZ2 : Crystal structure of the ''N. Clavipes'' spidroin NTD''' | '''5IZ2 : Crystal structure of the ''N. Clavipes'' spidroin NTD''' | ||
| - | 5IZ2 is the NTD domain of a protein called spidroin. This protein is a component of the dragline silk. | + | 5IZ2 is the NTD domain of a protein called spidroin[https://en.wikipedia.org/wiki/Spidroin]. This protein is a component of the dragline silk. |
There are several types of spidroin, and those that form the core of the silk are called '''MaSp1''' (Major ampullate Spidroin-1), which are produced by in the major ampullate gland of spiders. | There are several types of spidroin, and those that form the core of the silk are called '''MaSp1''' (Major ampullate Spidroin-1), which are produced by in the major ampullate gland of spiders. | ||
The NTD domain of these proteins is very important because it plays a major role in the dimerisation of spidroins. Indeed, thanks to the NTD organization, 2 spidroins can be combined, leading to the production of fibres with exceptional physical qualities. | The NTD domain of these proteins is very important because it plays a major role in the dimerisation of spidroins. Indeed, thanks to the NTD organization, 2 spidroins can be combined, leading to the production of fibres with exceptional physical qualities. | ||
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== Monomer structure of the spidroin NTD domain == | == Monomer structure of the spidroin NTD domain == | ||
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| + | One monomer of NTD is composed of 2 subunits, A and B, each of them composed of 5 α-helices. There is also a chain Z composed of 3 amino acids (Ser, Tyr, Gly), but it role is not well established yet. | ||
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| + | In each subunit, the orientation of helices 2, 3 and 5 is different from the orientation of helices 1 and 4. Indeed, helices 1 and 4 form the rigid body of the NTD domain, while helices 2, 3 and 5 are involved in intermolecular contacts, so they play an important role in the dimerization process. | ||
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| + | Moreover, at the opposite extremities of each subunits of the monomer there are clusters of acidic residus (Asp36, Asp39, Asp40, Glu79, Asp91) in one part, and clusters of basic residus (Lys54, Arg57, Lys60, Lys64, Lys65) in the other part. So, this create a dipole moment. And, as the subunits A and B are organized antiparallel, it allows an access to charges poles. | ||
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== Dimerization of the spidroin by the NTD domain == | == Dimerization of the spidroin by the NTD domain == | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
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| + | == Applications in Biotechnology == | ||
</StructureSection> | </StructureSection> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:49, 12 January 2020
| This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115. |
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5IZ2 : Crystal structure of the N. Clavipes spidroin NTD
5IZ2 is the NTD domain of a protein called spidroin[1]. This protein is a component of the dragline silk. There are several types of spidroin, and those that form the core of the silk are called MaSp1 (Major ampullate Spidroin-1), which are produced by in the major ampullate gland of spiders. The NTD domain of these proteins is very important because it plays a major role in the dimerisation of spidroins. Indeed, thanks to the NTD organization, 2 spidroins can be combined, leading to the production of fibres with exceptional physical qualities.
Contents |
Your Heading Here (maybe something like 'Structure')
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Global structure of the N. Clavipes Spidroin-1
Monomer structure of the spidroin NTD domain
One monomer of NTD is composed of 2 subunits, A and B, each of them composed of 5 α-helices. There is also a chain Z composed of 3 amino acids (Ser, Tyr, Gly), but it role is not well established yet.
In each subunit, the orientation of helices 2, 3 and 5 is different from the orientation of helices 1 and 4. Indeed, helices 1 and 4 form the rigid body of the NTD domain, while helices 2, 3 and 5 are involved in intermolecular contacts, so they play an important role in the dimerization process.
Moreover, at the opposite extremities of each subunits of the monomer there are clusters of acidic residus (Asp36, Asp39, Asp40, Glu79, Asp91) in one part, and clusters of basic residus (Lys54, Arg57, Lys60, Lys64, Lys65) in the other part. So, this create a dipole moment. And, as the subunits A and B are organized antiparallel, it allows an access to charges poles.
Dimerization of the spidroin by the NTD domain
|
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
Applications in Biotechnology
</StructureSection>
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
