YKL 40: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Safa Ahmed (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
==Structural Highlights== | ==Structural Highlights== | ||
<StructureSection load='' size='350' side='right' scene='88/881548/Ykl-40/1'> | <StructureSection load='' size='350' side='right' scene='88/881548/Ykl-40/1'> | ||
__TOC__ | |||
<scene name='88/881548/Ykl-40/1'>YKL-40</scene> is a non-enzymatic chitinase-like protein. It is able to bind chitin but does not possess the enzymatic activity needed to cleave chitinase. YKL-40 is the human form of chitinase-3 -like protein 1 also referred to as CHI3L1. It is referred to as YKL because of the three amino acid residues (Y, K, and L) present at the N terminus. The 40 comes from the weight of the protein which is around 40kDa. Previous crystallizations have shown a YKL-40 three-dimensional structure that consists of a (β/α)8- barrel domain. It also has a secondary domain comprised of six antiparallel β-strands with one α-helix (α + β) domain after β7. Full-length genomic chains can be observed in UniProt. The complete structure and 3D analysis can be found in the [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWR OCA atlas]. For a complete guided tour, [https://proteopedia.org/wiki/fgij/fg.htm?mol=1HJX FirstGlance] is recommended. | <scene name='88/881548/Ykl-40/1'>YKL-40</scene> is a non-enzymatic chitinase-like protein. It is able to bind chitin but does not possess the enzymatic activity needed to cleave chitinase. YKL-40 is the human form of chitinase-3 -like protein 1 also referred to as CHI3L1. It is referred to as YKL because of the three amino acid residues (Y, K, and L) present at the N terminus. The 40 comes from the weight of the protein which is around 40kDa. Previous crystallizations have shown a YKL-40 three-dimensional structure that consists of a (β/α)8- barrel domain. It also has a secondary domain comprised of six antiparallel β-strands with one α-helix (α + β) domain after β7. Full-length genomic chains can be observed in UniProt. The complete structure and 3D analysis can be found in the [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWR OCA atlas]. For a complete guided tour, [https://proteopedia.org/wiki/fgij/fg.htm?mol=1HJX FirstGlance] is recommended. | ||